Mutations probe structure and function of G-protein α chains

H. R. Bourne, S. B. Masters, R. T. Miller, K. A. Sullivan, W. Heideman

Research output: Contribution to journalArticlepeer-review


The molecular genetic approach has just begun to provide hints of answers to some of the questions posed at the outset of this paper. We have some idea of which portions of the α chain of G(s) interact with receptors and effectors, and we guess that the same is true of corresponding regions of other α chains. We have a tantalizing hint that points to a key region of α(s) that is necessary for the conformational change induced by binding GTP, and the vague outline of a hypothesis regarding the mechanism by which receptors release GDP from its binding site on the α chain. The α chain region (domain) that interacts with βγ remains unknown. The tenuous quality of all these hints and hypotheses is obvious, and at least in the short term, frustrating. Even the prevent level of our understanding, however, is impressive in comparison with what was known of G-protein function only 5 years ago. Now we can pose much more precise questions and hope that a combination of the molecular genetic approach with biophysical probes of structure will provide satisfying answers.

Original languageEnglish (US)
Pages (from-to)221-228
Number of pages8
JournalCold Spring Harbor symposia on quantitative biology
Issue number1
StatePublished - Jan 1 1988

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics


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