Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit
| Autor: | Heidi E. Hamm, Dusanka Deretic, Bernd Koenig, Klaus Hofmann, Anatol Arendt, Paul A. Hargrave |
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| Rok vydání: | 1988 |
| Předmět: |
Rhodopsin
genetic structures G protein Macromolecular Substances Protein Conformation Antigen-Antibody Complex GTP-Binding Proteins Protein A/G Amino Acid Sequence Transducin G alpha subunit G protein-coupled receptor kinase Multidisciplinary Binding Sites biology Chemistry Binding protein Antibodies Monoclonal Membrane Proteins Kinetics Biochemistry biology.protein sense organs Protein G Peptides Retinal Pigments Protein Binding |
| Zdroj: | Science (New York, N.Y.). 241(4867) |
| ISSN: | 0036-8075 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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