The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187.
Open accessAbstract
Cysteine residues 110 and 187 are essential for the formation of the correct bovine rhodopsin structure (Karnik, S. S., Sakmar, T. P., Chen, H.-B., and Khorana, H. G. (1988) Proc. Natl. Acad. Sci. U. S. A. 85, 8459-8463). We now show that the sulfhydryl groups of these 2 cysteine residues interact to form a disulfide bond. Rhodopsin mutants containing cysteine----serine substitutions were prepared as follows. In one mutant, CysVII, all the 10 cysteine residues of rhodopsin were replaced by serines. A second mutant, CysVIII, contained only C110 and C185; a third mutant, CysIX, contained only C185 and C187 while the fourth mutant, CysX, contained only C110 and C187. Only mutant CysX formed functional rhodopsin. Mutants CysVIII and CysIX reacted with [3H]iodoacetic acid showing the presence of free sulfhydryl groups while mutant CysX was inert to this reagent. CysX reacted with cyanide ion to form a thiocyanate derivative showing the presence of a disulfide bond. The C110-C187 disulfide bond is buried in rhodopsin because reactions with disulfide reducing agents and cyanide ion require prior treatment with denaturants.
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Cites
Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin
Dixon, R. A. F., Kobilka, B. K., Strader, D. J., Benovic, J. L., Dohlman, H. G., Frielle, T., Bolanowski, M. A., Bennett, C. D., Rands, E., Diehl, R. E., et al. (1986) · Nature · doi:10.1038/321075a0 · Cited by 1,276
Stryer, L. (1986) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.09.030186.000511 · Cited by 1,168
Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin
Nathans, J., & Hogness, D. S. (1983) · Cell · doi:10.1016/0092-8674(83)90537-8 · Cited by 701
Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin.
Sakmar, T. P., Franke, R. R., & Khorana, H. G. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.21.8309 · Cited by 679
Self-citationThe structure of bovine rhodopsin
Hargrave, P. A., McDowell, J. H., Curtis, D. R., Wang, J. K., Juszczak, E., Fong, S.-L., Mohana Rao, J. K., & Argos, P. (1983) · Biophysics of Structure and Mechanism · doi:10.1007/bf00535659 · Cited by 519
Expression of a synthetic bovine rhodopsin gene in monkey kidney cells.
Oprian, D. D., Molday, R. S., Kaufman, R. J., & Khorana, H. G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.8874 · Cited by 446
Self-citationKarnik, S. S., Sakmar, T. P., Chen, H. B., & Khorana, H. G. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.22.8459 · Cited by 414
Self-citationOvchinnikov, Y. A., Abdulaev, N. G., & Bogachuk, A. S. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80628-8 · Cited by 410
Three cytoplasmic loops of rhodopsin interact with transducin.
König, B., Arendt, A., McDowell, J. H., Kahlert, M., Hargrave, P. A., & Hofmann, K. P. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.18.6878 · Cited by 371
Structural features required for ligand binding to the beta-adrenergic receptor.
Dixon, R. A., Sigal, I. S., Candelore, M. R., Register, R. B., Scattergood, W., Rands, E., & Strader, C. D. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02645.x · Cited by 354
Cited by
Savarese, T. M., & Fraser, C. M. (1992) · Biochemical Journal · doi:10.1042/bj2830001 · Cited by 473
Rhodopsin: Structural Basis of Molecular Physiology
Menon, S. T., Han, M., & Sakmar, T. P. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.4.1659 · Cited by 304
G Protein-Coupled Receptor Rhodopsin: A Prospectus
Filipek, S., Stenkamp, R. E., Teller, D. C., & Palczewski, K. (2003) · Annual Review of Physiology · doi:10.1146/annurev.physiol.65.092101.142611 · Cited by 267
Rhodopsin: Insights from Recent Structural Studies
Sakmar, T. P., Menon, S. T., Marin, E. P., & Awad, E. S. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.082901.134348 · Cited by 240
Retinal counterion switch in the photoactivation of the G protein-coupled receptor rhodopsin
Yan, E. C. Y., Kazmi, M. A., Ganim, Z., Hou, J.-M., Pan, D., Chang, B. S. W., Sakmar, T. P., & Mathies, R. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1531970100 · Cited by 197
Metadata
- Authors
- Karnik, S. S., & Khorana, H. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-10
- Volume
- 265
- Issue
- 29
- Pages
- 17520-17524
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1584684122
- Cited by
- 314
- References
- 21
- FWCI
- 6.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
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