Article
Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state.
Proceedings of the National Academy of Sciences of the United States of America - 23 Dec 1997
Kim J M, Altenbach C, Thurmond R L, Khorana H G, Hubbell W L
Abstract excerpt
The Glu-134-Arg-135 residues in rhodopsin, located near the cytoplasmic end of the C helix, are involved in G protein binding, or activation, or both. Furthermore, the charge-neutralizing mutation Glu-134 to Gln-134 produces hyperactivity in the activated state and produces constitutive activity in opsin. The Glu/Asp-Arg charge pair is highly conserved in equivalent positions in other G protein-coupled receptors....
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.