Xiangrong Liu and Fengjuan Li contributed equally to this work.
Solution structure of the SH3 domain of DOCK180†
Article first published online: 25 FEB 2013
Copyright © 2013 Wiley Periodicals, Inc.
Proteins: Structure, Function, and Bioinformatics
Volume 81, Issue 5, pages 906–910, May 2013
How to Cite
Liu, X., Li, F., Pan, Z., Wang, W. and Wen, W. (2013), Solution structure of the SH3 domain of DOCK180. Proteins, 81: 906–910. doi: 10.1002/prot.24236
- Issue published online: 4 APR 2013
- Article first published online: 25 FEB 2013
- Accepted manuscript online: 13 DEC 2012 05:47AM EST
- Manuscript Accepted: 28 NOV 2012
- Manuscript Revised: 9 NOV 2012
- Manuscript Received: 17 AUG 2012
- National Major Basic Research Program. Grant Numbers: 2009CB918600, 2011CB808505
- National Science Foundation of China. Grant Numbers: 30970574, 31270778, 20973040, 31070642
- Shanghai Rising-Star Program. Grant Number: 10QA1400700
- Science and Technology Commission of Shanghai Municipality. Grant Number: 08DZ2270500
- atypical SH3;
- NMR spectroscopy;
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. Proteins 2013. © 2012 Wiley Periodicals, Inc.