Proteopedia - User contributions [en]

Sandbox Reserved 1654

2021-01-13T20:28:42Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB ([https://en.wikipedia.org/wiki/CPEB1 CPEB1] to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns'''<ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Zinc finger domain' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins. Therefore, it is this area that would be a platform to bind different proteins (ePAB, PARN, ...) by making hydrogen bonds.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRMs' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other:
***<scene name='86/868187/Rmm/4'>RRM1</scene> has anti-parallel beta strands between the <scene name='86/868187/Rmm/7'>alpha helix</scene> and the <scene name='86/868187/Rmm/8'>beta4 strand</scene>.
***The <scene name='86/868187/Rmm/10'>interdomain linker</scene> takes a helical turn that interacts with residues of the N-terminal extension and with <scene name='86/868187/Rmm/6'>RRM2</scene>.
***<scene name='86/868187/Rmm/1'>Trp331</scene> positions RRM2 relative to RRM1 by inserting between the beta sheet and <scene name='86/868187/Rmm/9'>alpha1 helix</scene> of RRM2.
***After the helical turn, the interdomain linker folds in a <scene name='86/868187/Rmm/11'>beta strand</scene> which is anti-parallel to the <scene name='86/868187/Rmm/12'>beta2 strand</scene> (RRM2). The interdomain linker is therefore a kind of joint for the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between [https://en.wikipedia.org/wiki/Senescence senescence] and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the [https://en.wikipedia.org/wiki/Cytoplasmic_polyadenylation_element CPE] sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase [https://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease PARN] which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the [https://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase poly(A) polymerase] which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-12T14:12:14Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB ([https://en.wikipedia.org/wiki/CPEB1 CPEB1] to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns'''<ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Zinc finger domain' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRMs' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other:
***<scene name='86/868187/Rmm/4'>RRM1</scene> has anti-parallel beta strands between the <scene name='86/868187/Rmm/7'>alpha helix</scene> and the <scene name='86/868187/Rmm/8'>beta4 strand</scene>.
***The <scene name='86/868187/Rmm/10'>interdomain linker</scene> takes a helical turn that interacts with residues of the N-terminal extension and with <scene name='86/868187/Rmm/6'>RRM2</scene>.
***<scene name='86/868187/Rmm/1'>Trp331</scene> positions RRM2 relative to RRM1 by inserting between the beta sheet and <scene name='86/868187/Rmm/9'>alpha1 helix</scene> of RRM2.
***After the helical turn, the interdomain linker folds in a <scene name='86/868187/Rmm/11'>beta strand</scene> which is anti-parallel to the <scene name='86/868187/Rmm/12'>beta2 strand</scene> (RRM2). The interdomain linker is therefore a kind of joint for the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between [https://en.wikipedia.org/wiki/Senescence senescence] and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the [https://en.wikipedia.org/wiki/Cytoplasmic_polyadenylation_element CPE] sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase [https://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease PARN] which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the [https://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase poly(A) polymerase] which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-12T14:10:43Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB ([https://en.wikipedia.org/wiki/CPEB1 CPEB1] to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns'''<ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Zinc finger domain' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRMs' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other:
***<scene name='86/868187/Rmm/4'>RRM1</scene> has anti-parallel beta strands between the <scene name='86/868187/Rmm/7'>alpha helix</scene> and the <scene name='86/868187/Rmm/8'>beta4 strand</scene>.
***The <scene name='86/868187/Rmm/10'>interdomain linker</scene> takes a helical turn that interacts with residues of the N-terminal extension and with <scene name='86/868187/Rmm/6'>RRM2</scene>.
***<scene name='86/868187/Rmm/1'>Trp331</scene> positions RRM2 relative to RRM1 by inserting between the beta sheet and <scene name='86/868187/Rmm/9'>alpha1 helix</scene> of RRM2.
***After the helical turn, the interdomain linker folds in a <scene name='86/868187/Rmm/11'>beta strand</scene> which is anti-parallel to the <scene name='86/868187/Rmm/12'>beta2 strand</scene> (RRM2). The interdomain linker is therefore a kind of joint for the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between [https://en.wikipedia.org/wiki/Senescence senescence] and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the [https://en.wikipedia.org/wiki/Cytoplasmic_polyadenylation_element CPE] sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase [https://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease PARN] which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the [https://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase poly(A) polymerase] which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-11T17:56:57Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns'''<ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
***RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
***Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
***Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. ***After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-11T17:56:17Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns'''<ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
***RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
***Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
***Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. ***After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

<scene name='86/868187/Slt/2'>bonjour</scene>

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T14:22:19Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns'''<ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T14:20:01Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : 2 RRMs domains and zinc finger domains.
** '''Zinc finger patterns'''<ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T14:19:41Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : 2 RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''<ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T14:18:54Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind<ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA<ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : 2 RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T14:17:53Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind <ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA <ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : 2 RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref name="publi" />. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref name="publi" />.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T14:17:23Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind <ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA <ref name="publi">DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : 2 RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publi" />.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too[2]. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation[2].

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T14:13:49Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind <ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA <ref>DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : 2 RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<up>[2]</up>.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too[2]. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation[2].

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T14:11:30Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind <ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA <ref>DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : 2 RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA[2].
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too[2]. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation[2].

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T14:09:55Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind <ref name="publi" />DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA <ref name="publica" />DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : 2 RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref name="publica" />.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too[2]. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation[2].

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T13:58:30Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind <ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA <ref>DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : 2 RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==
CPEB controls the balance between senescence and proliferation. Indeed, due to its two structural domains in its C-terminal region, it has the capacity to modify mRNA<ref>DOI 10.1016/j.arr.2012.03.004</ref>.
RRMs domains allow binding to the CPE sequence of mRNA (pyrimidine rich : UUUUUAU), thus ensuring good RNA positioning and high fidelity.
Zing finger domains allow binding to different proteins, which play a role in affinity but not in specificity. It's therefore its ability to recruit different proteins that will determine its action, activation or repression of translation.

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too<ref>DOI 10.1016/j.arr.2012.03.004</ref>. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation<ref>DOI 10.1016/j.arr.2012.03.004</ref>.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-10T13:50:19Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==
[https://en.wikipedia.org/wiki/CPEB CPEB ](Cytoplasmic polyadenylation element binding protein) is present in most vertebrates and invertebrates and can activate or inhibit translation, depending on the different factors it can bind <ref>DOI 10.1016/j.tibs.2007.04.004</ref>. In human body there are 4 different isoforms of CPEB (CPEB1 to CPEB4), distributed throughout body in a tissue-dependent manner and which interact differently with mRNA <ref>DOI 10.1016/j.arr.2012.03.004</ref>.
CPEB protein regulates the length of the polyA tail which allows to control the translation. It binds to mRNA and in association with some factors, can act as a translational repressor or activator, depending on these factors.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : 2 RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>
<StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
</StructureSection>
RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.

== Function ==

A specific arrangement of CPEs in mRNA can lead to the repression of the translation. In this case, the CPEB can form a dimer which could avoid the bound of the polyA polymerase complex in 2 different ways. It could prevent the association of ePAB with the polyA tail because CPEB recruits the deadenylase PARN which reduce the length of the polyA tail. It could disrupt the interaction between the binding factors of the translation [https://en.wikipedia.org/wiki/EIF4E eIF4E] and [https://en.wikipedia.org/wiki/EIF4G eIF4G] too, because CPEB recruits the protein Maskin which blocks eIF4G recruitment too. This prevents the bound of the cap machinery to the mRNA and therefore inhibits the translation.

On the other hand, the CPEB can activate the translation. Indeed, in the cytoplasm, there are some repressed or silenced mRNA with a short polyA tail. They can be activated by cytoplasmic polyadenylation thanks to a hormonal stimulation. This stimulation can lead to the phosphorylation of CPEB which increase its affinity with the [https://en.m.wikipedia.org/wiki/Cleavage_and_polyadenylation_specificity_factor CPSF] (Cleavage and Polyadenylation Specificity Factor) and decrease the binding between CPEB and PARN. CPSF binds to the mRNA at the sequence 3’ of the tail of the mRNA (AAUAAA) and recruits the poly(A) polymerase which leads to the elongation of the polyA tail and therefore to the activation of the translation.

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T13:14:59Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytoplasmic Polyadenylation Element-Binding Protein (CPEB)==

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>

== Function ==

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T13:14:31Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>

== Function ==

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T13:14:08Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133.114</ref>

== Function ==

== Disease ==

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T13:12:33Z

Sarah Stadnik:

Sandbox Reserved 1654

2021-01-08T13:08:12Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T12:55:04Z

Sarah Stadnik:

Sandbox Reserved 1654

2021-01-08T12:53:15Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/j.jmb.2013.03.009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T12:51:51Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns'''
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133114</ref>

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T12:51:11Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/jjmb.201303009</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133114</ref>

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T12:48:37Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/ijch.201303024</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns''' <ref>DOI 10.1101/gad.241133114</ref>

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T12:45:30Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns''' <ref>DOI 10.1016/ijch.201303024</ref>
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T12:37:42Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns'''
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines involved in a bond with a zinc atom, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-08T11:19:10Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns : RRMs domains and zinc finger domains.
** '''Zinc finger patterns'''
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-07T10:14:45Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** '''Zinc finger patterns'''
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T19:45:37Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** '''Zinc finger patterns'''
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A <scene name='86/868187/310/1'>310 helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T19:44:00Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** '''Zinc finger patterns'''
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A <scene name='86/868187/310/1'>310 helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/1'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T19:31:28Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** '''Zinc finger patterns'''
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A <scene name='86/868187/310/1'>310 helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/2'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/1'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T19:20:54Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** '''Zinc finger patterns'''
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. <scene name='86/868187/Zz/3'>The domain</scene> includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A <scene name='86/868187/310/1'>310 helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/1'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/1'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T19:18:24Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All <scene name='86/868187/Zz/3'>CPEB proteins</scene> have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** '''Zinc finger patterns'''
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A <scene name='86/868187/310/1'>310 helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/1'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/1'>Cys527, Cys532, His545 and His553</scene>.
** '''RRMs patterns'''

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T19:13:11Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** '''Zinc finger patterns'''
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A <scene name='86/868187/310/1'>310 helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/1'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/1'>Cys527, Cys532, His545 and His553</scene>.
** RRMs patterns

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T19:12:06Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** Zinc finger patterns
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A <scene name='86/868187/310/1'>310 helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/1'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/1'>Cys527, Cys532, His545 and His553</scene>.
** RRMs patterns

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T19:04:00Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** Zinc finger patterns
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes :
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An α1 helix (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 helical turn (residues 550-552).
***2 zinc binding sites, the first one is composed of Cys515, Cys518, Cys537, Cys540 and the second is composed of Cys527, Cys532, His545 and His553.
** RRMs patterns

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T18:37:23Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** Zinc finger patterns
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes :
***A Rubredoxin turn (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An α1 helix (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 helical turn (residues 550-552).
***2 zinc binding sites, the first one is composed of Cys515, Cys518, Cys537, Cys540 and the second is composed of Cys527, Cys532, His545 and His553.
** RRMs patterns

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T18:36:03Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** Zinc finger patterns
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes :
***A Rubredoxin turn (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An α1 helix (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 helical turn (residues 550-552).
***2 zinc binding sites, the first one is composed of Cys515, Cys518, Cys537, Cys540 and the second is composed of Cys527, Cys532, His545 and His553.
** RRMs patterns

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T18:35:44Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** Zinc finger patterns
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes : ***A Rubredoxin turn (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An α1 helix (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 helical turn (residues 550-552).
***2 zinc binding sites, the first one is composed of Cys515, Cys518, Cys537, Cys540 and the second is composed of Cys527, Cys532, His545 and His553.
** RRMs patterns

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T18:35:07Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** Zinc finger patterns
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes :
***A Rubredoxin turn (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An α1 helix (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 helical turn (residues 550-552).
***2 zinc binding sites, the first one is composed of Cys515, Cys518, Cys537, Cys540 and the second is composed of Cys527, Cys532, His545 and His553.
** RRMs patterns

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T18:34:35Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).
** Zinc finger patterns
<StructureSection load='2m13' size='340' side='left' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes :
***A Rubredoxin turn (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An α1 helix (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 helical turn (residues 550-552).
***2 zinc binding sites, the first one is composed of Cys515, Cys518, Cys537, Cys540 and the second is composed of Cys527, Cys532, His545 and His553.

** RRMs patterns

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T18:32:48Z

Sarah Stadnik:

{{Sandbox_Reserved_ESBS20_}}
==Cytplasmic Polyadenylation Element-binding Protein (CPEB)==

You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Structure ==
All CPEB proteins have a similar structure :
* A N-terminal region which is a regulatory region with phosphorylation and dephosphorylation sites. This region is variable in length and composition.
* A C-terminal region, composed of 2 recognition patterns (RRMs which allow a good positioning of RNA, a high fidelity and are essential for the CPE specific recognition) and 2 zinc finger patterns (containing two zinc binding sites and a specific RNA-binding protein sequence which play a role in affinity but not in specificity).

** Zinc finger patterns
<StructureSection load='2m13' size='340' side='right' caption='Caption for this structure' scene=''>
</StructureSection>
About 54 residues with 6 cysteines and 2 histidines, conserved for all isoforms and species. The modification of one of the eight zinc ligands destabilize the connection to the mRNA. The domain includes :
***A Rubredoxin turn (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with β1 (residues 525-527) and β2 (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An α1 helix (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***A 310 helical turn (residues 550-552).
***2 zinc binding sites, the first one is composed of Cys515, Cys518, Cys537, Cys540 and the second is composed of Cys527, Cys532, His545 and His553.

** RRMs patterns

== Function ==

== Disease ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

== References ==
<references/>

Sandbox Reserved 1654

2021-01-03T18:15:37Z

Sarah Stadnik:

Sandbox Reserved 1654

2021-01-03T18:14:11Z

Sarah Stadnik:

Sandbox Reserved 1654

2021-01-03T18:13:19Z

Sarah Stadnik:

Sandbox Reserved 1654

2021-01-03T18:12:35Z

Sarah Stadnik:

Sandbox Reserved 1654

2021-01-03T18:12:10Z

Sarah Stadnik:

Sandbox Reserved 1654

2021-01-03T18:11:33Z

Sarah Stadnik: