The structure of the GTPase-activating domain from p50rhoGAP

Tracey Barrett, Bing Xiao, Eleanor J. Dodson, Guy Dodson, Steven B. Ludbrook, Kurshid Nurmahomed, Steven J. Gamblin, Andrea Musacchio, Stephen J. Smerdon and John F. Eccleston
Additional contact information
Tracey Barrett: National Institute for Medical Research
Bing Xiao: National Institute for Medical Research
Eleanor J. Dodson: University of York
Guy Dodson: National Institute for Medical Research
Steven B. Ludbrook: National Institute for Medical Research
Kurshid Nurmahomed: National Institute for Medical Research
Steven J. Gamblin: National Institute for Medical Research
Andrea Musacchio: Childrens Hospital
Stephen J. Smerdon: National Institute for Medical Research
John F. Eccleston: National Institute for Medical Research

Nature, 1997, vol. 385, issue 6615, 458-461

Abstract: Abstract Members of the Rho family of small G proteins transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation1–4. They also activate other kinase cascades. Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form5. The active conformation is promoted by guanine-nucleotide exchange factors, and the inactive state by GTPase-activating proteins (GAPs) which stimulate the intrinsic GTPase activity of small G proteins6. Rho-specific GAP domains are found in a wide variety of large, multi-functional proteins7. Here we report the crystal structure of an active 242-residue C-terminal fragment of human p50rhoGAP8. The structure is an unusual arrangement of nine α-helices, the core of which includes a four-helix bundle. Residues conserved across the rhoGAP family are largely confined to one face of this bundle, which may be an interaction site for target G proteins. In particular, we propose that Arg 85 and Asn 194 are involved in binding G proteins and enhancing GTPase activity.

Date: 1997
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/385458a0 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:385:y:1997:i:6615:d:10.1038_385458a0

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/385458a0

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().