Linked Life Data

9545299

Source:http://linkedlifedata.com/resource/pubmed/id/9545299

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1998-5-21
pubmed:databankReference
pubmed:abstractText
The 2.4-A resolution crystal structure of a dominantly active form of the small guanosine triphosphatase (GTPase) RhoA, RhoAV14, complexed with the nonhydrolyzable GTP analogue, guanosine 5'-3-O-(thio)triphosphate (GTPgammaS), reveals a fold similar to RhoA-GDP, which has been recently reported (Wei, Y., Zhang, Y., Derewenda, U., Liu, X., Minor, W., Nakamoto, R. K., Somlyo, A. V., Somlyo, A. P., and Derewenda, Z. S. (1997) Nat. Struct. Biol. 4, 699-703), but shows large conformational differences localized in switch I and switch II. These changes produce hydrophobic patches on the molecular surface of switch I, which has been suggested to be involved in its effector binding. Compared with H-Ras and other GTPases bound to GTP or GTP analogues, the significant conformational differences are located in regions involving switches I and II and part of the antiparallel beta-sheet between switches I and II. Key residues that produce these conformational differences were identified. In addition to these differences, RhoA contains four insertion or deletion sites with an extra helical subdomain that seems to be characteristic of members of the Rho family, including Rac1, but with several variations in details. These sites also display large displacements from those of H-Ras. The ADP-ribosylation residue, Asn41, by C3-like exoenzymes stacks on the indole ring of Trp58 with a hydrogen bond to the main chain of Glu40. The recognition of the guanosine moiety of GTPgammaS by the GTPase contains water-mediated hydrogen bonds, which seem to be common in the Rho family. These structural differences provide an insight into specific interaction sites with the effectors, as well as with modulators such as guanine nucleotide exchange factor (GEF) and guanine nucleotide dissociation inhibitor (GDI).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9656-66
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9545299-Amino Acid Sequence, pubmed-meshheading:9545299-Binding Sites, pubmed-meshheading:9545299-Cloning, Molecular, pubmed-meshheading:9545299-Computer Simulation, pubmed-meshheading:9545299-Conserved Sequence, pubmed-meshheading:9545299-Crystallography, X-Ray, pubmed-meshheading:9545299-GTP Phosphohydrolases, pubmed-meshheading:9545299-GTP-Binding Proteins, pubmed-meshheading:9545299-Guanosine 5'-O-(3-Thiotriphosphate), pubmed-meshheading:9545299-Guanosine Triphosphate, pubmed-meshheading:9545299-Humans, pubmed-meshheading:9545299-Models, Molecular, pubmed-meshheading:9545299-Molecular Sequence Data, pubmed-meshheading:9545299-Mutagenesis, Site-Directed, pubmed-meshheading:9545299-Point Mutation, pubmed-meshheading:9545299-Protein Conformation, pubmed-meshheading:9545299-Protein Structure, Secondary, pubmed-meshheading:9545299-Recombinant Proteins, pubmed-meshheading:9545299-Sequence Alignment, pubmed-meshheading:9545299-Sequence Homology, Amino Acid, pubmed-meshheading:9545299-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:9545299-rhoA GTP-Binding Protein
pubmed:year
1998
pubmed:articleTitle
Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue.
pubmed:affiliation
Divisions of Structural Biology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-01, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't