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| [[Image:1oeb.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1oeb| PDB=1oeb | SCENE= }} | | {{STRUCTURE_1oeb| PDB=1oeb | SCENE= }} |
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| '''MONA/GADS SH3C DOMAIN'''
| | ===MONA/GADS SH3C DOMAIN=== |
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| ==Overview==
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| SH3 domains are protein recognition modules within many adaptors and enzymes. With more than 500 SH3 domains in the human genome, binding selectivity is a key issue in understanding the molecular basis of SH3 domain interactions. The Grb2-like adaptor protein Mona/Gads associates stably with the T-cell receptor signal transducer SLP-76. The crystal structure of a complex between the C-terminal SH3 domain (SH3C) of Mona/Gads and a SLP-76 peptide has now been solved to 1.7 A. The peptide lacks the canonical SH3 domain binding motif P-x-x-P and does not form a frequently observed poly-proline type II helix. Instead, it adopts a clamp-like shape around the circumfence of the SH3C beta-barrel. The central R-x-x-K motif of the peptide forms a 3(10) helix and inserts into a negatively charged double pocket on the SH3C while several other residues complement binding through hydrophobic interactions, creating a short linear SH3C binding epitope of uniquely high affinity. Interestingly, the SH3C displays ion-dependent dimerization in the crystal and in solution, suggesting a novel mechanism for the regulation of SH3 domain functions.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12773374}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12773374 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12773374}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Signal tranduction]] | | [[Category: Signal tranduction]] |
| [[Category: Slp-76]] | | [[Category: Slp-76]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:44:09 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:54:16 2008'' |
