1oeb: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1oeb]] is a 4 chain structure with 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=1OEB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OEB FirstGlance]. <br> | <table><tr><td colspan='2'>[[1oeb]] is a 4 chain structure with 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=1OEB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OEB FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h3h|1h3h]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h3h|1h3h]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1oeb RCSB], [http://www.ebi.ac.uk/pdbsum/1oeb PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1oeb RCSB], [http://www.ebi.ac.uk/pdbsum/1oeb PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/LCP2_MOUSE LCP2_MOUSE]] Involved in T-cell antigen receptor mediated signaling.<ref>PMID:10660534</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Bourette, R P | [[Category: Bourette, R P]] | ||
[[Category: Feller, S M | [[Category: Feller, S M]] | ||
[[Category: Gilbert, R J.C | [[Category: Gilbert, R J.C]] | ||
[[Category: Harkiolaki, M | [[Category: Harkiolaki, M]] | ||
[[Category: Jones, E Y | [[Category: Jones, E Y]] | ||
[[Category: Lewitzky, M | [[Category: Lewitzky, M]] | ||
[[Category: Moarefi, I | [[Category: Moarefi, I]] | ||
[[Category: Mouchiroud, G | [[Category: Mouchiroud, G]] | ||
[[Category: Sondermann, H | [[Category: Sondermann, H]] | ||
[[Category: Dimer]] | [[Category: Dimer]] | ||
[[Category: Gad]] | [[Category: Gad]] | ||
Revision as of 10:06, 25 December 2014
MONA/GADS SH3C DOMAINMONA/GADS SH3C DOMAIN
Structural highlights
Function[LCP2_MOUSE] Involved in T-cell antigen receptor mediated signaling.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSH3 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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