The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Local peptide movement in the photoreaction intermediate of rhodopsin
Abstract
Photoactivation of the visual rhodopsin, a prototypical G protein-coupled receptor (GPCR), involves efficient conversion of the intrinsic inverse-agonist 11- cis -retinal to the all - trans agonist. This event leads to the rearrangement of the heptahelical transmembrane bundle, which is thought to be shared by hundreds of GPCRs. To examine this activation mechanism, we determined the x-ray crystallographic model of the photoreaction intermediate of rhodopsin, lumirhodopsin, which represents the conformational state having the nearly complete all - trans agonist form of the retinal. A difference electron density map clearly indicated that the distorted all - trans -retinal in the precedent intermediate bathorhodopsin relaxes by dislocation of the β-ionone ring in lumirhodopsin, along with significant peptide displacement in the middle of helix III, including approximately two helical turns. This local movement results in the breaking of the electrostatic interhelical restraints mediated by many of the conserved residues among rhodopsin-like GPCRs, with consequent acquisition of full activity.
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Citations
Cites
Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637
Self-citationThe Retinal Conformation and its Environment in Rhodopsin in Light of a New 2.2 Å Crystal Structure
Okada, T., Sugihara, M., Bondar, A.-N., Elstner, M., Entel, P., & Buss, V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.044 · Cited by 1,049
Self-citationRetinal 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
Crystal structure of rhodopsin: implications for vision and beyond
Okada, T. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00227-x · Cited by 121
Self-citation
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
Crystal structure of metarhodopsin II
Choe, H.-W., Kim, Y. J., Park, J. H., Morizumi, T., Pai, E. F., Krauß, N., Hofmann, K. P., Scheerer, P., & Ernst, O. P. (2011) · Nature · doi:10.1038/nature09789 · Cited by 663
Normal Mode Analysis of Biomolecular Structures: Functional Mechanisms of Membrane Proteins
Bahar, I., Lezon, T. R., Bakan, A., & Shrivastava, I. H. (2010) · Chemical Reviews · doi:10.1021/cr900095e · Cited by 537
Action of Molecular Switches in GPCRs - Theoretical and Experimental Studies
Trzaskowski, B., Latek, D., Yuan, S., Ghoshdastider, U., Debinski, A., & Filipek, S. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712799320556 · Cited by 469
Crystal structure of a photoactivated deprotonated intermediate of rhodopsin
Salom, D., Lodowski, D. T., Stenkamp, R. E., Trong, I. L., Golczak, M., Jastrzebska, B., Harris, T., Ballesteros, J. A., & Palczewski, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608022103 · Cited by 442
Metadata
- Authors
- Nakamichi, H., & Okada, T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-08-22
- Volume
- 103
- Issue
- 34
- Pages
- 12729-12734
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2112329754
- Cited by
- 203
- References
- 4
- FWCI
- 7.86
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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