Proteopedia - User contributions [en]

Stepler sandbox STAT3

2015-12-18T12:52:32Z

Cameron Stepler:

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
STAT3 (Signal Transducer and Activator of Transcription 3) is one of a family of seven homologous STAT proteins that differentially regulate gene expression. STAT 3 is important in both the development of embryos and many functions in adult organisms. <ref>PMID:11050435</ref>

== Structure ==
The STAT3 protein is composed of several <scene name='71/714950/Stat3_helix_turn_helix/1'>Helix Turn Helix</scene> structures and its quaternary structure consists of two STAT3 proteins <scene name='71/714950/Stat3_dimer/1'>dimerized</scene> with themselves. <ref>PMID:9671298</ref>

== Regulation ==
STAT3 plays a large role in differential gene regulation. One way that STAT3 can regulate gene expression is through protein-protein interactions with other transcription factors. One major protein-protein interaction for STAT3 is the interaction with nF-κB p65. <ref>PMID:14978160</ref> <scene name='71/714950/Nf-kb_binding_domain/1'>The nF-κB p65 binding domain (yellow)</scene> is characterized by the β-pleated sheet structures. Other protein transcription factors have been shown to interact with STAT3 in similar ways at different locations. STAT3 can also be regulated by phosphorylation. There is a <scene name='71/714950/Important_c-terminal_y_residue/1'>Y residue</scene> at the C-terminal that plays a large role in transcriptional activation during regulatory events. Phosphorylation of the transcription activating domain's Y residue can be used as a regulatory process. Alternatively, other sites can also be phosphorylated causing other regulatory pathways to occur, such as serine phosphorylation and oncogene activity from STAT3. <ref>PMID:22418867</ref>

== DNA-Protein Interactions ==
The <scene name='71/714950/Stat3_dimer_and_dna/1'>STAT3 protein dimer interacts with DNA</scene> by "clamping" around it. <scene name='71/714950/Dna-binding_domain/4'>STAT3 residues bind to DNA</scene> by interacting with the major groove of it. STAT3 (along with other STAT family members) bind to specific DNA sequences. <ref>PMID:11050435</ref> STAT3 has a binding domain with sequences like <scene name='71/714950/Dna-binding_domain_dna_portion/1'>TTN(5-6)AA</scene>. <scene name='71/714950/Dna-binding_domain/3'>This stretch</scene> is then what interacts with the STAT3 protein. As shown in the scene, the DNA is bound by the protein in its major groove. Positively charged glutamines and lysines interact with the negatively charged phosphates of the DNA. This is what allows to the protein to bind in the major groove.

</StructureSection>
== References ==
<references/>

Stepler sandbox STAT3

2015-12-18T12:48:08Z

Cameron Stepler:

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
STAT3 (Signal Transducer and Activator of Transcription 3) is one of a family of seven homologous STAT proteins that differentially regulate gene expression. STAT 3 is important in both the development of embryos and many functions in adult organisms. <ref>PMID:11050435</ref>

== Structure ==
The STAT3 protein is composed of several <scene name='71/714950/Stat3_helix_turn_helix/1'>Helix Turn Helix</scene> structures and its quaternary structure consists of two STAT3 proteins <scene name='71/714950/Stat3_dimer/1'>dimerized</scene> with themselves. <ref>PMID:9671298</ref>

== Regulation ==
STAT3 plays a large role in differential gene regulation. One way that STAT3 can regulate gene expression is through protein-protein interactions with other transcription factors. One major protein-protein interaction for STAT3 is the interaction with nF-κB p65. <ref>PMID:14978160</ref> <scene name='71/714950/Nf-kb_binding_domain/1'>The nF-κB p65 binding domain (yellow)</scene> is characterized by the β-pleated sheet structures. Other protein transcription factors have been shown to interact with STAT3 in similar ways at different locations. STAT3 can also be regulated by phosphorylation. There is a <scene name='71/714950/Important_c-terminal_y_residue/1'>Y residue</scene> at the C-terminal that plays a large role in transcriptional activation during regulatory events. Phosphorylation of the transcription activating domain's Y residue can be used as a regulatory process. Alternatively, other sites can also be phosphorylated causing other regulatory pathways to occur, such as serine phosphorylation and oncogene activity from STAT3. <ref>PMID:22418867</ref>

== DNA-Protein Interactions ==
The <scene name='71/714950/Stat3_dimer_and_dna/1'>STAT3 protein dimer interacts with DNA</scene> by "clamping" around it. <scene name='71/714950/Dna-binding_domain/4'>STAT3 residues bind to DNA</scene> by interacting with the major groove of it. STAT3 (along with other STAT family members) bind to specific DNA sequences. <ref>PMID:11050435</ref> STAT3 has a binding domain with sequences like <scene name='71/714950/Dna-binding_domain_dna_portion/1'>TTN(5-6)AA</scene>. <scene name='71/714950/Dna-binding_domain/3'>This stretch</scene> is then what interacts with the STAT3 protein. As shown in the scene, the DNA is bound by the protein in its major groove. This occurs via hydrogen bonding between the amino acids and the nucleotide bases.

</StructureSection>
== References ==
<references/>

Stepler sandbox STAT3

2015-12-18T12:47:07Z

Cameron Stepler:

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
STAT3 (Signal Transducer and Activator of Transcription 3) is one of a family of seven homologous STAT proteins that differentially regulate gene expression. STAT 3 is important in both the development of embryos and many functions in adult organisms. <ref>PMID:11050435</ref>

== Structure ==
The STAT3 protein is composed of several <scene name='71/714950/Stat3_helix_turn_helix/1'>Helix Turn Helix</scene> structures and its quaternary structure consists of two STAT3 proteins <scene name='71/714950/Stat3_dimer/1'>dimerized</scene> with themselves. <ref>PMID:9671298</ref>

== Regulation ==
STAT3 plays a large role in differential gene regulation. One way that STAT3 can regulate gene expression is through protein-protein interactions with other transcription factors. One major protein-protein interaction for STAT3 is the interaction with nF-κB p65. <ref>PMID:14978160</ref> <scene name='71/714950/Nf-kb_binding_domain/1'>The nF-κB p65 binding domain (yellow)</scene> is characterized by the β-pleated sheet structures. Other protein transcription factors have been shown to interact with STAT3 in similar ways at different locations. STAT3 can also be regulated by phosphorylation. There is a <scene name='71/714950/Important_c-terminal_y_residue/1'>Y residue</scene> at the C-terminal that plays a large role in transcriptional activation during regulatory events. Phosphorylation of the transcription activating domain's Y residue can be used as a regulatory process. Alternatively, other sites can also be phosphorylated causing other regulatory pathways to occur, such as serine phosphorylation and oncogene activity from STAT3. <ref>PMID:22418867</ref>

== DNA-Protein Interactions ==
The <scene name='71/714950/Stat3_dimer_and_dna/1'>STAT3 protein dimer interacts with DNA</scene> by "clamping" around it. <scene name='71/714950/Dna-binding_domain/4'>Stat3 residues bind to DNA</scene> by interacting with the major groove of it. STAT3 (along with other STAT family members) bind to specific DNA sequences. <ref>PMID:11050435</ref> STAT3 has a binding domain with sequences like <scene name='71/714950/Dna-binding_domain_dna_portion/1'>TTN(5-6)AA</scene>. <scene name='71/714950/Dna-binding_domain/3'>This stretch</scene> is then what interacts with the STAT3 protein. As shown in the scene, the DNA is bound by the protein in its major groove. This occurs via hydrogen bonding between the amino acids and the nucleotide bases.

</StructureSection>
== References ==
<references/>

Stepler sandbox STAT3

2015-12-18T12:42:04Z

Cameron Stepler:

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
STAT3 (Signal Transducer and Activator of Transcription 3) is one of a family of seven homologous STAT proteins that differentially regulate gene expression. STAT 3 is important in both the development of embryos and many functions in adult organisms. <ref>PMID:11050435</ref>

== Structure ==
The STAT3 protein is composed of several <scene name='71/714950/Stat3_helix_turn_helix/1'>Helix Turn Helix</scene> structures and its quaternary structure consists of two STAT3 proteins <scene name='71/714950/Stat3_dimer/1'>dimerized</scene> with themselves. <ref>PMID:9671298</ref>

== Regulation ==
STAT3 plays a large role in differential gene regulation. One way that STAT3 can regulate gene expression is through protein-protein interactions with other transcription factors. One major protein-protein interaction for STAT3 is the interaction with nF-κB p65. <ref>PMID:14978160</ref> <scene name='71/714950/Nf-kb_binding_domain/1'>The nF-κB p65 binding domain (yellow)</scene> is characterized by the β-pleated sheet structures. Other protein transcription factors have been shown to interact with STAT3 in similar ways at different locations. STAT3 can also be regulated by phosphorylation. There is a <scene name='71/714950/Important_c-terminal_y_residue/1'>Y residue</scene> at the C-terminal that plays a large role in transcriptional activation during regulatory events. Phosphorylation of the transcription activating domain's Y residue can be used as a regulatory process. Alternatively, other sites can also be phosphorylated causing other regulatory pathways to occur, such as serine phosphorylation and oncogene activity from STAT3. <ref>PMID:22418867</ref>

== DNA-Protein Interactions ==
The <scene name='71/714950/Stat3_dimer_and_dna/1'>STAT3 protein dimer interacts with DNA</scene> by "clamping" around it. <scene name='71/714950/Dna-binding_domain/4'>Stat3 residues bind to DNA</scene> by interacting with the major groove of it. STAT3 (along with other STAT family members) bind to specific DNA sequences. <ref>PMID:11050435</ref> STAT3 has a binding domain with sequences like TTN(5-6)AA. <scene name='71/714950/Dna-binding_domain/3'>This stretch</scene> is then what interacts with the STAT3 protein. As shown in the scene, the DNA is bound by the protein in its major groove.

</StructureSection>
== References ==
<references/>

Stepler sandbox STAT3

2015-12-18T12:40:41Z

Cameron Stepler:

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
STAT3 (Signal Transducer and Activator of Transcription 3) is one of a family of seven homologous STAT proteins that differentially regulate gene expression. STAT 3 is important in both the development of embryos and many functions in adult organisms. <ref>PMID:11050435</ref>

== Structure ==
The STAT3 protein is composed of several <scene name='71/714950/Stat3_helix_turn_helix/1'>Helix Turn Helix</scene> structures and its quaternary structure consists of two STAT3 proteins <scene name='71/714950/Stat3_dimer/1'>dimerized</scene> with themselves. <ref>PMID:9671298</ref>

== Regulation ==
STAT3 plays a large role in differential gene regulation. One way that STAT3 can regulate gene expression is through protein-protein interactions with other transcription factors. One major protein-protein interaction for STAT3 is the interaction with nF-κB p65. <ref>PMID:14978160</ref> <scene name='71/714950/Nf-kb_binding_domain/1'>The nF-κB p65 binding domain (yellow)</scene> is characterized by the β-pleated sheet structures. Other protein transcription factors have been shown to interact with STAT3 in similar ways at different locations. STAT3 can also be regulated by phosphorylation. There is a <scene name='71/714950/Important_c-terminal_y_residue/1'>Y residue</scene> at the C-terminal that plays a large role in transcriptional activation during regulatory events. Phosphorylation of the transcription activating domain's Y residue can be used as a regulatory process. Alternatively, other sites can also be phosphorylated causing other regulatory pathways to occur, such as serine phosphorylation and oncogene activity from STAT3. <ref>PMID:22418867</ref>

== DNA-Protein Interactions ==
The <scene name='71/714950/Stat3_dimer_and_dna/1'>STAT3 protein dimer interacts with DNA</scene> by wrapping around it. <scene name='71/714950/Dna-binding_domain/4'>Stat3 interacts with DNA</scene> by binding to the major groove of it. STAT3 (along with other STAT family members) bind to specific DNA sequences. <ref>PMID:11050435</ref> STAT3 has a binding domain with sequences like TTN(5-6)AA. <scene name='71/714950/Dna-binding_domain/3'>This stretch</scene> is then what interacts with the STAT3 protein. As shown in the scene, the DNA is bound by the protein in its major groove.

</StructureSection>
== References ==
<references/>

Stepler sandbox STAT3

2015-12-18T12:18:51Z

Cameron Stepler:

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
STAT3 (Signal Transducer and Activator of Transcription 3) is one of a family of seven homologous STAT proteins that differentially regulate gene expression. STAT 3 is important in both the development of embryos and many functions in adult organisms. <ref>PMID:11050435</ref>

== Structure ==
The STAT3 protein is composed of several <scene name='71/714950/Stat3_helix_turn_helix/1'>Helix Turn Helix</scene> structures and its quaternary structure consists of two STAT3 proteins <scene name='71/714950/Stat3_dimer/1'>dimerized</scene> with themselves. <ref>PMID:9671298</ref> There is a <scene name='71/714950/Important_c-terminal_y_residue/1'>Y residue</scene> at the C-terminal that plays a large role in transcriptional activation during regulatory events.

== Regulation ==
STAT3 plays a large role in differential gene regulation. One way that STAT3 can regulate gene expression is through protein-protein interactions with other transcription factors. One major protein-protein interaction for STAT3 is the interaction with nF-κB p65. <ref>PMID:14978160</ref> <scene name='71/714950/Nf-kb_binding_domain/1'>The nF-κB p65 binding domain (yellow)</scene> is characterized by the β-pleated sheet structures. Other protein transcription factors have been shown to interact with STAT3 in similar ways at different locations. STAT3 can also be regulated by phosphorylation. There is a <scene name='71/714950/Important_c-terminal_y_residue/1'>Y residue</scene> at the C-terminal that plays a large role in transcriptional activation during regulatory events. Phosphorylation of the transcription activating domain's Y residue can be used as a regulatory process. Alternatively, other sites can also be phosphorylated causing other regulatory pathways to occur, such as serine phosphorylation and oncogene activity from STAT3. <ref>PMID:22418867</ref>

== DNA-Protein Interactions ==
The <scene name='71/714950/Stat3_dimer_and_dna/1'>STAT3 protein interacts with DNA</scene> by binding to the major groove of the DNA. STAT3 (along with other STAT family members) bind to specific DNA sequences. <ref>PMID:11050435</ref> STAT3 has a binding domain with sequences like TTN(5-6)AA. <scene name='71/714950/Dna-binding_domain/3'>This stretch</scene> is then what interacts with the STAT3 protein. As shown in the scene, the DNA is bound by the protein in its major groove.

</StructureSection>
== References ==
<references/>

Stepler sandbox STAT3

2015-10-13T12:32:20Z

Cameron Stepler:

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
STAT3 (Signal Transducer and Activator of Transcription 3) is one of seven of a family of homologous STAT proteins that differentially regulate gene expression. STAT 3 is important in both the development of embryos and many functions in adult organisms. <ref>PMID:11050435</ref>

== Structure ==
The STAT3 protein is composed of several helix-turn-helix structures and its quaternary structure consists of two STAT3 proteins dimerized with themselves. <ref>PMID:9671298</ref> There is a <scene name='71/714950/Important_c-terminal_y_residue/1'>Y residue</scene> at the C-terminal that plays a large role in transcriptional activation during regulatory events.

== Regulation ==
STAT3 plays a large role in differential gene regulation. One way that STAT3 can regulate gene expression is through protein-protein interactions with other transcription factors. One major protein-protein interaction for STAT3 is the interaction with nF-κB p65. <ref>PMID:14978160</ref> <scene name='71/714950/Nf-kb_binding_domain/1'>The nF-κB p65 binding domain</scene> is characterized by the β-pleated sheet structures. Other protein transcription factors have been shown to interact with STAT3 in similar ways at different locations. STAT3 can also be regulated by phosphorylation. Phosphorylation of the transcription activating domain's Y residue can be used as a regulatory process. Alternatively, other sites can also be phosphorylated causing other regulatory pathways to occur, such as serine phosphorylation and oncogene activity from STAT3. <ref>PMID:22418867</ref>

== DNA-Protein Interactions ==
The <scene name='71/714950/Stat3_dimer_and_dna/1'>STAT3 protein interacts with DNA</scene> by binding to the major groove of the DNA. STAT3 (along with other STAT family members) bind to specific DNA sequences. <ref>PMID:11050435</ref> STAT3 has a binding domain with sequences like TTN(5-6)AA. <scene name='71/714950/Dna-binding_domain/3'>This stretch</scene> is then what interacts with the STAT3 protein. As shown in the scene, the DNA is bound by the protein in its major groove.

</StructureSection>
== References ==
<references/>

Stepler sandbox STAT3

2015-10-13T06:16:35Z

Cameron Stepler:

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
STAT3 (Signal Transducer and Activator of Transcription 3) is one of seven of a family of homologous STAT proteins that differentially regulate gene expression. STAT 3 is important in both the development of embryos and many functions in adult organisms. <ref>PMID:11050435</ref>

== Structure ==
The STAT3 protein is composed of several helix-turn-helix structures and its quaternary structure consists of two STAT3 proteins dimerized with themselves. <ref>PMID:9671298</ref> There is a <scene name='71/714950/Important_c-terminal_y_residue/1'>Y residue</scene> at the C-terminal that plays a large role in transcriptional activation during regulatory events.

== Regulation ==
STAT3 plays a large role in differential gene regulation. One way that STAT3 can regulate gene expression is through protein-protein interactions with other transcription factors. One major protein-protein interaction for STAT3 is the interaction with nF-κB p65. <ref>PMID:14978160</ref> <scene name='71/714950/Nf-kb_binding_domain/1'>The nF-κB p65 binding domain</scene> is characterized by the β-pleated sheet structures. Other protein transcription factors have been shown to interact with STAT3 in similar ways at different locations. STAT3 can also be regulated by phosphorylation. Phosphorylation of the transcription activating domain's Y residue can be used as a regulatory process. Alternatively, other sites can also be phosphorylated causing other regulatory pathways to occur, such as serine phosphorylation and oncogene activity from STAT3. <ref>PMID:22418867</ref>

== DNA-Protein Interactions ==
The <scene name='71/714950/Stat3_dimer_and_dna/1'>STAT3 protein interacts with DNA</scene> by binding to the major groove of the DNA. STAT3 (along with other STAT family members) bind to specific DNA sequences. <ref>PMID:11050435</ref> STAT3 has a binding domain with sequences like TTN(5-6)AA. <scene name='71/714950/Dna-binding_domain/1'>This stretch</scene> is then what interacts with the STAT3 protein. As shown in the scene, the DNA is bound by the protein in its major groove.

</StructureSection>
== References ==
<references/>

Stepler sandbox STAT3

2015-10-13T05:20:20Z

Cameron Stepler:

Stepler sandbox STAT3

2015-10-13T04:45:09Z

Cameron Stepler:

Stepler sandbox STAT3

2015-10-13T04:36:03Z

Cameron Stepler:

Stepler sandbox STAT3

2015-10-13T03:54:04Z

Cameron Stepler:

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
This is a default text for your page '''Stepler sandbox STAT3'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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 STAT3 <ref>PMID:9671298</ref> to the rescue.

== Structure ==
<scene name='71/714950/Stat3_dimer_and_dna/1'>TextToBeDisplayed</scene>

== Regulation ==

== DNA-Protein Interactions ==

== Structural highlights ==

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.

</StructureSection>
== References ==
<references/>

File:1bg1 mm1.pdb

2015-10-06T13:24:37Z

Cameron Stepler: The biological unit of STAT3 made with makeMultimer.py.

== Summary ==
The biological unit of STAT3 made with makeMultimer.py.
== Licensing ==
{{subst:No license from license selector|Don't know}}

Stepler sandbox STAT3

2015-10-06T12:33:54Z

Cameron Stepler:

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
This is a default text for your page '''Stepler sandbox STAT3'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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 STAT3 <ref>PMID:9671298</ref> to the rescue.

== Structure ==

== Regulation ==

== DNA-Protein Interactions ==

== Structural highlights ==

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.

</StructureSection>
== References ==
<references/>

Stepler sandbox STAT3

2015-10-06T12:31:42Z

Cameron Stepler: New page: ==STAT3== <StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''> This is a default text for your page '''Stepler sandbox STAT3'''. Click above...

==STAT3==
<StructureSection load='1bg1' size='340' side='right' caption='STAT3 Interacting with DNA' scene=''>
This is a default text for your page '''Stepler sandbox STAT3'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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 STAT3 <ref>PMID:9671298</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

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.

</StructureSection>
== References ==
<references/>