2M0Y

Solution structure of the SH3 domain of DOCK180

Summary for 2M0Y

• Entry DOI: 10.2210/pdb2m0y/pdb
• NMR Information: BMRB: 18832
• Descriptor: Dedicator of cytokinesis protein 1 (1 entity in total)
• Functional Keywords: apoptosis
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm (By similarity): Q8BUR4
• Total number of polymer chains: 1
• Total formula weight: 8659.84

Authors

Liu, X.,Wen, W. (deposition date: 2012-11-08, release date: 2012-12-19, Last modification date: 2024-05-15)

Primary citation

Liu, X.,Li, F.,Pan, Z.,Wang, W.,Wen, W.
Solution structure of the SH3 domain of DOCK180.
Proteins, 81:906-910, 2013

PubMed Abstract: DOCK180 family proteins are Rho guanine nucleotide exchange factors. DOCK1-5 contains an N-terminal SH3 domain implicated in their autoinhibition. Release of the closed conformation requires the interaction between SH3 and engulfment and cell motility (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.

PubMed: 23239367
DOI: 10.1002/prot.24236

Experimental method

SOLUTION NMR