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Site of G Protein Binding to Rhodopsin Mapped with Synthetic Peptides from the α Subunit
Abstract
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 α subunit, Glu 311 -Val 328 and Ile 340 -Phe 350 , compete with G protein for interaction with rhodopsin. Amino acid substitution studies show that Cys 321 is required for this effect. Ile 340 -Phe 350 and a modified peptide, acetyl-Glu 311 -Lys 329 -amide, mimic G protein effects on rhodopsin conformation, showing that these peptides bind to and stabilize the activated conformation of rhodopsin.
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Citations
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Self-citationMechanistic insights into G-protein coupling with an agonist-bound G-protein-coupled receptor
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Mechanism of G‐protein Activation by Rhodopsin†
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Metadata
- Authors
- Hamm, H. E., Deretic, D., Arendt, A., Hargrave, P. A., Koenig, B., & Hofmann, K. P.
- Venue
- Science
- Published
- 1988-08-12
- Volume
- 241
- Issue
- 4867
- Pages
- 832-835
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2015176049
- Cited by
- 498
- References
- 0
- FWCI
- 6.48
- Type
- journal article
- Language
- en
- Open access
- closed
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