Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit.

Hamm HE, Deretic D, Arendt A, Hargrave PA, Koenig B, Hofmann KP
Science. 1988 241 (4867): 832-5

PMID: 3136547 · DOI:10.1126/science.3136547

The interaction between receptors and guanine nucleotide binding (G) proteins leads to G protein activation and subsequent regulation of effector enzymes. The molecular basis of receptor-G protein interaction has been examined by using the ability of the G protein from rods (transducin) to cause a conformational change in rhodopsin as an assay. Synthetic peptides corresponding to two regions near the carboxyl terminus of the G protein alpha subunit, Glu311-Val328 and Ile340-Phe350, compete with G protein for interaction with rhodopsin. Amino acid substitution studies show that Cys321 is required for this effect. Ile340-Phe350 and a modified peptide, acetyl-Glu311-Lys329-amide, mimic G protein effects on rhodopsin conformation, showing that these peptides bind to and stabilize the activated conformation of rhodopsin.

MeSH Terms (14)

Amino Acid Sequence Antibodies, Monoclonal Antigen-Antibody Complex Binding Sites GTP-Binding Proteins Kinetics Macromolecular Substances Membrane Proteins Peptides Protein Binding Protein Conformation Retinal Pigments Rhodopsin Transducin

Connections (1)

This publication is referenced by other Labnodes entities: