4did
From Proteopedia
Crystal structure of Salmonella effector N-terminal domain SopB in complex with Cdc42
Structural highlights
Function[CDC42_HUMAN] Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration.[1] [2] [3] Publication Abstract from PubMedSopB is a Type III secreted Salmonella effector protein with phosphoinositide phosphatase activity and a GTPase binding domain that 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. Structure of Salmonella Effector Protein SopB N-terminal domain in complex with Host Rho GTPase Cdc42.,Burkinshaw B, Strynadka NC J Biol Chem. 2012 Feb 23. PMID:22362774[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||
