The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Rhodopsin Mutants That Bind But Fail to Activate Transducin
Abstract
Rhodopsin is a member of a family of receptors that contain seven transmembrane helices and are coupled to G proteins. The nature of the interactions between rhodopsin mutants and the G protein, transducin (G t), was investigated by flash photolysis in order to monitor directly G t binding and dissociation. Three mutant opsins with alterations in their cytoplasmic loops bound 11-cis-retinal to yield pigments with native rhodopsin absorption spectra, but they failed to stimulate the guanosine triphosphatase activity of G t. The opsin mutations included reversal of a charged pair conserved in all G protein-coupled receptors at the cytoplasmic border of the third transmembrane helix (mutant CD1), replacement of 13 amino acids in the second cytoplasmic loop (mutant CD2), and deletion of 13 amino acids from the third cytoplasmic loop (mutant EF1). Whereas mutant CD1 failed to bind G t, mutants CD2 and EF1 showed normal G t binding but failed to release G t in the presence of guanosine triphosphate. Therefore, it appears that at least the second and third cytoplasmic loops of rhodopsin are required for activation of bound G t.
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Cites
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Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin
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Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin.
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Self-citationThe structure of bovine rhodopsin
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Cited by
Crystal structure of opsin in its G-protein-interacting conformation
Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059
Self-citationStructure and dynamics of GPCR signaling complexes
Hilger, D., Masureel, M., & Kobilka, B. K. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0011-7 · Cited by 969
Savarese, T. M., & Fraser, C. M. (1992) · Biochemical Journal · doi:10.1042/bj2830001 · Cited by 473
Rhodopsin, photoreceptor of the rod cell. An emerging pattern for structure and function.
Khorana, H. G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48444-x · Cited by 434
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Metadata
- Authors
- Franke, R. R., König, B., Sakmar, T. P., Khorana, H. G., & Hofmann, K. P.
- Venue
- Science
- Published
- 1990-10-05
- Volume
- 250
- Issue
- 4977
- Pages
- 123-125
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1993343824
- Cited by
- 377
- References
- 24
- FWCI
- 9.86
- Type
- journal article
- Language
- en
- Open access
- closed
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- Franke, R. R., König, B., Sakmar, T. P., Khorana, H. G., & Hofmann, K. P. (1990). Rhodopsin Mutants That Bind But Fail to Activate Transducin. Science. https://doi.org/10.1126/science.2218504
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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