2bbu
From Proteopedia
(New page: 200px<br /><applet load="2bbu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bbu" /> '''solution structure of mouse socs3 in complex...) |
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| - | [[Image:2bbu.gif|left|200px]]<br /><applet load="2bbu" size=" | + | [[Image:2bbu.gif|left|200px]]<br /><applet load="2bbu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bbu" /> | caption="2bbu" /> | ||
'''solution structure of mouse socs3 in complex with a phosphopeptide from the gp130 receptor'''<br /> | '''solution structure of mouse socs3 in complex with a phosphopeptide from the gp130 receptor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | SOCS3 is essential for regulating the extent, duration, and specificity of | + | SOCS3 is essential for regulating the extent, duration, and specificity of cellular responses to cytokines such as G-CSF and IL-6. Here we describe the solution structure of SOCS3, the first structure determined for any SOCS protein, in complex with a phosphotyrosine-containing peptide from the IL-6 receptor signaling subunit gp130. The structure of the complex shows that seven peptide residues form a predominantly hydrophobic binding motif. Regions outside the SOCS3 SH2 domain are important for ligand binding, in particular, a single 15 residue alpha helix immediately N-terminal to the SH2 domain makes direct contacts with the phosphotyrosine binding loop and, in part, determines its geometry. The SH2 domain itself is remarkable in that it contains a 35 residue unstructured PEST motif insertion that is not required for STAT inhibition. The PEST motif increases SOCS3 turnover and affects its degradation pathway, implying that it has an important regulatory role inside the cell. |
==About this Structure== | ==About this Structure== | ||
| - | 2BBU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 2BBU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BBU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Babon, J | + | [[Category: Babon, J J.]] |
| - | [[Category: Norton, R | + | [[Category: Norton, R S.]] |
[[Category: Yao, S.]] | [[Category: Yao, S.]] | ||
[[Category: extended sh2 subdomain]] | [[Category: extended sh2 subdomain]] | ||
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[[Category: sh2 domain]] | [[Category: sh2 domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:07 2008'' |
Revision as of 14:36, 21 February 2008
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solution structure of mouse socs3 in complex with a phosphopeptide from the gp130 receptor
Overview
SOCS3 is essential for regulating the extent, duration, and specificity of cellular responses to cytokines such as G-CSF and IL-6. Here we describe the solution structure of SOCS3, the first structure determined for any SOCS protein, in complex with a phosphotyrosine-containing peptide from the IL-6 receptor signaling subunit gp130. The structure of the complex shows that seven peptide residues form a predominantly hydrophobic binding motif. Regions outside the SOCS3 SH2 domain are important for ligand binding, in particular, a single 15 residue alpha helix immediately N-terminal to the SH2 domain makes direct contacts with the phosphotyrosine binding loop and, in part, determines its geometry. The SH2 domain itself is remarkable in that it contains a 35 residue unstructured PEST motif insertion that is not required for STAT inhibition. The PEST motif increases SOCS3 turnover and affects its degradation pathway, implying that it has an important regulatory role inside the cell.
About this Structure
2BBU is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability., Babon JJ, McManus EJ, Yao S, DeSouza DP, Mielke LA, Sprigg NS, Willson TA, Hilton DJ, Nicola NA, Baca M, Nicholson SE, Norton RS, Mol Cell. 2006 Apr 21;22(2):205-16. PMID:16630890
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