Ontology highlight
ABSTRACT:
SUBMITTER: Stiegler AL
PROVIDER: S-EPMC9722645 | biostudies-literature | 2022 Dec
REPOSITORIES: biostudies-literature
Stiegler Amy L AL Vish Kimberly J KJ Boggon Titus J TJ
Structure (London, England : 1993) 20221122 12
p120RasGAP is a multidomain GTPase-activating protein for Ras. The presence of two Src homology 2 domains in an SH2-SH3-SH2 module raises the possibility that p120RasGAP simultaneously binds dual phosphotyrosine residues in target proteins. One known binding partner with two proximal phosphotyrosines is p190RhoGAP, a GTPase-activating protein for Rho GTPases. Here, we present the crystal structure of the p120RasGAP SH2-SH3-SH2 module bound to a doubly tyrosine-phosphorylated p190RhoGAP peptide, ...[more]