Abstract
The guanosine triphosphate-binding proteins (G proteins) found in a variety of tissues transduce signals generated by ligand binding to cell surface receptors into changes in intracellular metabolism. Amino acid sequences of peptides prepared by partial proteolysis of the α subunit of a bovine brain G protein and the α subunit of rod outer-segment transducin were determined. The two proteins show regions of sequence identity as well as regions of diversity. A portion of the amino-terminal peptide sequence of each protein is highly homologous with the corresponding region in the ras protein (a protooncogene product). These similarities suggest that G proteins and ras proteins may have analogous functions.
Original language | English (US) |
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Pages (from-to) | 860-862 |
Number of pages | 3 |
Journal | Science |
Volume | 226 |
Issue number | 4676 |
DOIs | |
State | Published - 1984 |
ASJC Scopus subject areas
- General