Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-08

AUTHORS

Katrin Rittinger, Philip A. Walker, John F. Eccleston, Kurshid Nurmahomed, Darerca Owen, Ernest Laue, Steven J. Gamblin, Stephen J. Smerdon

ABSTRACT

Small G proteins transduce signals from plasma-membrane receptors to control a wide range of cellular functions. These proteins are clustered into distinct families but all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of G proteins, which includes Cdc42Hs, activate effectors involved in the regulation of cytoskeleton formation, cell proliferation and the JNK signalling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GTPase-activating proteins (GAPs) that enhance the rate of GTP hydrolysis by up to 10(5) times. We report here the crystal structure of Cdc42Hs, with the non-hydrolysable GTP analogue GMPPNP, in complex with the GAP domain of p50rhoGAP at 2.7A resolution. In the complex Cdc42Hs interacts, mainly through its switch I and II regions, with a shallow pocket on rhoGAP which is lined with conserved residues. Arg 85 of rhoGAP interacts with the P-loop of Cdc42Hs, but from biochemical data and by analogy with the G-protein subunit G(i alpha1), we propose that it adopts a different conformation during the catalytic cycle which enables it to stabilize the transition state of the GTP-hydrolysis reaction. More... »

PAGES

693-697

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/41805

DOI

http://dx.doi.org/10.1038/41805

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1000815147

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9262406


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