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- PLoS ONE 2020-12;
Crystal structures of p120RasGAP N-terminal SH2 domain in its apo form and in complex with a p190RhoGAP phosphotyrosine peptide
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A synthetic 13 amino acid peptide of sequence EEENI(p-Tyr)SVPHDST native to p190RhoGAP residues 1100 to 1112 phosphorylated at Tyr-1105, with N-terminal acetylation and C-terminal amidation, was commercially synthesized (GenScript) and re-suspended in sterile-filtered water. | |
AbstractThe Rho and Ras pathways play vital roles in cell growth, division and motility. Cross-talk between the pathways amplifies their roles in cell proliferation and motility and its dysregulation is involved in disease pathogenesis. One important interaction for cross-talk occurs between p120RasGAP (RASA1), a GTPase activating protein (GAP) for Ras, and p190RhoGAP (p190RhoGAP-A, ARHGAP35), a GAP for Rho. The binding of these proteins is primarily mediated by two SH2 domains within p120RasGAP engaging phosphorylated tyrosines of p190RhoGAP, of which the best studied is pTyr-1105. To better understand the interaction between p120RasGAP and p190RhoGAP, we determined the 1.75 Å X-ray crystal structure of the N-termina... More KeywordsMost Popular Services |