Structural highlights
Function
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).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu X, Li F, Pan Z, Wang W, Wen W. Solution structure of the SH3 domain of DOCK180. Proteins. 2012 Dec 13. doi: 10.1002/prot.24236. PMID:23239367 doi:http://dx.doi.org/10.1002/prot.24236
