Sandbox Reserved 1654: Difference between revisions

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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.

* 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>

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***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>

~~==Your Heading Here (maybe something like 'Structure')==~~

</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 ==

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@@ Line 6: / Line 6: @@
 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.
+* 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=''>
@@ Line 17: / Line 17: @@
 ***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>
-==Your Heading Here (maybe something like 'Structure')==
 <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 ==