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Science 10 November 1995:
Vol. 270. no. 5238, p. 933
DOI: 10.1126/science.270.5238.933
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Perspectives

Henry R. Bourne

H. Bourne comments on an unusual polymeric crystal structure for the alpha subunit of the heterotrimeric G protein presented in this issue of Science by Mixon et al. (p. 954). Although he questions the authors' suggestion that Galpha might exist as a polymer in the cell, he shows how a domain consisting of the amino and carboxyl terminal ends of the protein, evident in the polymeric structure, may be revealing how Galpha catalyzes GTP-GDP exchange.

The author is in the Department of Cellular and Molecular Pharmacology and Medicine, Cardiovascular Research Institute and the Cell Biology Program, University of California, San Francisco, CA 94143-0450, USA. E-mail: h_bourne.pcol@quickmail.ucsf.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Receptor-independent Activation of Atrial Muscarinic Potassium Channels in the Absence of Nucleotides.
A. S. Otero, L. Xu, Y. Ni, and G. Szabo (1998)
J. Biol. Chem. 273, 28868-28872
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alpha Helix Content of G Protein alpha  Subunit Is Decreased upon Activation by Receptor Mimetics.
T. Tanaka, T. Kohno, S.'i. Kinoshita, H. Mukai, H. Itoh, M. Ohya, T. Miyazawa, T. Higashijima, and K. Wakamatsu (1998)
J. Biol. Chem. 273, 3247-3252
   Abstract »    Full Text »    PDF »


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