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1oeb
From Proteopedia
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| - | [[Image:1oeb.gif|left|200px]] | + | [[Image:1oeb.gif|left|200px]] |
| - | + | ||
| - | '''MONA/GADS SH3C DOMAIN''' | + | {{Structure |
| + | |PDB= 1oeb |SIZE=350|CAPTION= <scene name='initialview01'>1oeb</scene>, resolution 1.76Å | ||
| + | |SITE= <scene name='pdbsite=CD1:Cd+Binding+Site+For+Chain+A'>CD1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MONA/GADS SH3C DOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OEB is a [ | + | 1OEB is a [[Protein complex]] structure of sequences 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=1OEB OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76., Harkiolaki M, Lewitzky M, Gilbert RJ, Jones EY, Bourette RP, Mouchiroud G, Sondermann H, Moarefi I, Feller SM, EMBO J. 2003 Jun 2;22(11):2571-82. PMID:[http:// | + | Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76., Harkiolaki M, Lewitzky M, Gilbert RJ, Jones EY, Bourette RP, Mouchiroud G, Sondermann H, Moarefi I, Feller SM, EMBO J. 2003 Jun 2;22(11):2571-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12773374 12773374] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: CD]] | [[Category: CD]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
| - | [[Category: | + | [[Category: gad]] |
[[Category: mona]] | [[Category: mona]] | ||
[[Category: sh3]] | [[Category: sh3]] | ||
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[[Category: slp-76]] | [[Category: slp-76]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:09:38 2008'' |
Revision as of 11:09, 20 March 2008
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| , resolution 1.76Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MONA/GADS SH3C DOMAIN
Overview
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.
About this Structure
1OEB is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76., Harkiolaki M, Lewitzky M, Gilbert RJ, Jones EY, Bourette RP, Mouchiroud G, Sondermann H, Moarefi I, Feller SM, EMBO J. 2003 Jun 2;22(11):2571-82. PMID:12773374
Page seeded by OCA on Thu Mar 20 13:09:38 2008
Categories: Mus musculus | Protein complex | Bourette, R P. | Feller, S M. | Gilbert, R J.C. | Harkiolaki, M. | Jones, E Y. | Lewitzky, M. | Moarefi, I. | Mouchiroud, G. | Sondermann, H. | CD | Dimer | Gad | Mona | Sh3 | Signal tranduction | Slp-76
