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PMID: 9302995 Published · ppublish English Letter Research Support, U.S. Gov't, P.H.S.

Crystal structure of RhoA-GDP and its functional implications.

Nature structural biology ·Vol. 4 ·No. 9 ·1997-09-00 ·Pages 699-703

Wei Y, Zhang Y, Derewenda U, Liu X, Minor W, Nakamoto RK, Somlyo AV, Somlyo AP, Derewenda ZS

Abstract

RhoA, a ubiquitous intracellular GTPase, mediates cytoskeletal responses to extracellular signals. A 2.1 A resolution crystal structure of the human RhoA-GDP complex shows unique stereochemistry in the switch I region, which results in a novel mode of Mg2+ binding.

MeSH Terms
Crystallography, X-Ray GTP-Binding Proteins/chemistry,metabolism Guanosine Diphosphate/chemistry,metabolism Humans Magnesium/chemistry Models, Molecular Protein Conformation rhoA GTP-Binding Protein
Chemicals
Guanosine Diphosphate GTP-Binding Proteins rhoA GTP-Binding Protein Magnesium
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Wei Y
Zhang Y
Derewenda U
Liu X
Minor W
Nakamoto R K
Somlyo A V
Somlyo A P
Derewenda Z S
Article Info
Journal
Nature structural biology
Abbr.
Nat Struct Biol
ISSN
1072-8368
DOI
10.1038/nsb0997-699
Published
1997-09-00
Pages
699-703
Language
English
Region
United States
NLM ID
9421566
Subset
IM
Grants
NHLBI NIH HHS · P01 HL048807 · United States
External Links
PubMed source DOI: 10.1038/nsb0997-699
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