Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 16, Pages 13348-13355Publisher
ELSEVIER
DOI: 10.1074/jbc.M111.331330
Keywords
-
Categories
Funding
- Canadian Institute for Health Research
- Canadian Foundation of Innovation
- British Columbia Knowledge Development Fund
- Natural Sciences and Engineering Research Council of Canada
Ask authors/readers for more resources
SopB is a type III secreted Salmonella effector protein with phosphoinositide phosphatase activity and a distinct GTPase binding domain. The latter interacts with host Cdc42, an essential Rho GTPase that regulates critical events in eukaryotic cytoskeleton organization and membrane trafficking. Structural and biochemical analysis of the SopB GTPase binding domain in complex with Cdc42 shows for the first time that SopB structurally and functionally mimics a host guanine nucleotide dissociation inhibitor (GDI) by contacting key residues in the regulatory switch regions of Cdc42 and slowing Cdc42 nucleotide exchange.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available