1oeb
From Proteopedia
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|PDB= 1oeb |SIZE=350|CAPTION= <scene name='initialview01'>1oeb</scene>, resolution 1.76Å | |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> | |SITE= <scene name='pdbsite=CD1:Cd+Binding+Site+For+Chain+A'>CD1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oeb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oeb OCA], [http://www.ebi.ac.uk/pdbsum/1oeb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oeb RCSB]</span> | ||
}} | }} | ||
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[[Category: Mouchiroud, G.]] | [[Category: Mouchiroud, G.]] | ||
[[Category: Sondermann, H.]] | [[Category: Sondermann, H.]] | ||
| - | [[Category: CD]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
[[Category: gad]] | [[Category: gad]] | ||
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[[Category: slp-76]] | [[Category: slp-76]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:44:02 2008'' |
Revision as of 19:44, 30 March 2008
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| , resolution 1.76Å | |||||||
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| Sites: | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 22:44:02 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. | Dimer | Gad | Mona | Sh3 | Signal tranduction | Slp-76
