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Cited by 190

The DOI matches its Crossref record; 71 of the 71 references it cites were found in a registry or an index.

Crystal Structure of Human RhoA in a Dominantly Active Form Complexed with a GTP Analogue

Ihara, Kentaro, Muraguchi, Sachiko, Kato, Masato, Shimizu, Toshiyuki, Shirakawa, Masahiro, Kuroda, Shinya, Kaibuchi, Kozo, Hakoshima, Toshio·1998·Journal of Biological Chemistry
DOI 10.1074/jbc.273.16.9656
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Abstract

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 con…

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Crossref · 10.1074/jbc.273.16.9656

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Citations

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Show all 71 references

Research works printed but not linked: 2

  1. Self, 1993, Oncogene, 8, 655
  2. Kaibuchi, 1991, Mol. Cell. Biol., 11, 2873

Cited by

Metadata

Authors
Ihara, K., Muraguchi, S., Kato, M., Shimizu, T., Shirakawa, M., Kuroda, S., Kaibuchi, K., & Hakoshima, T.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-04
Volume
273
Issue
16
Pages
9656-9666
ISSN
0021-9258
DOI
10.1074/jbc.273.16.9656
Cited by
190
References
71
Language
en
Licence

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