2m0y
From Proteopedia
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| - | {{STRUCTURE_2m0y| PDB=2m0y | SCENE= }} | ||
| - | ===Solution structure of the SH3 domain of DOCK180=== | ||
| - | {{ABSTRACT_PUBMED_23239367}} | ||
| - | == | + | ==Solution structure of the SH3 domain of DOCK180== |
| - | [[http://www.uniprot.org/uniprot/DOCK1_MOUSE DOCK1_MOUSE | + | <StructureSection load='2m0y' size='340' side='right'caption='[[2m0y]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2m0y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M0Y FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m0y OCA], [https://pdbe.org/2m0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m0y RCSB], [https://www.ebi.ac.uk/pdbsum/2m0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m0y ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DOCK1_MOUSE DOCK1_MOUSE] Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1 (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | DOCK180 family proteins are Rho guanine nucleotide exchange factors (GEFs). DOCK1-5 contain an N-terminal SH3 domain implicated in their autoinhibition. Release of the closed conformation requires the interaction between SH3 and ELMO. Here we solved the solution structure of DOCK180 SH3 domain, which shares similar target binding features with the SH3 domain of DOCK2. The conserved N-terminal extension packs with the SH3 core domain and forms a new target binding site distinct from the canonical "PxxP" site. Our results demonstrate that the bidentate target binding mode of DOCK180 SH3 domain might be a general feature in all DOCK proteins. Proteins 2012. (c) 2012 Wiley Periodicals, Inc. | ||
| - | + | Solution structure of the SH3 domain of DOCK180.,Liu X, Li F, Pan Z, Wang W, Wen W Proteins. 2012 Dec 13. doi: 10.1002/prot.24236. PMID:23239367<ref>PMID:23239367</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2m0y" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Dedicator of cytokinesis protein 3D structures|Dedicator of cytokinesis protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Liu | + | [[Category: Liu X]] |
| - | [[Category: Wen | + | [[Category: Wen W]] |
| - | + | ||
Current revision
Solution structure of the SH3 domain of DOCK180
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