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Trends Biochem Sci. 2003 Sep;28(9):479-87.

Phototransduction: crystal clear.

Author information

1
Center for Advanced Research in Biotechnology, National Institute of Standards and Technology and the University of Maryland Biotechnology Institute,Rockville, MD 20850, USA. ridge@carb.nist.gov

Erratum in

  • Trends Biochem Sci. 2003 Oct;28(10):526.

Abstract

Vertebrate visual phototransduction represents one of the best-characterized G-protein-coupled receptor-mediated signaling pathways. Structural analyses of rhodopsin, G protein, arrestin and several other phototransduction components have revealed common folds and motifs that are important for function. Static and dynamic information has been acquired through the application of X-ray diffraction, solution and solid-state nuclear magnetic resonance spectroscopy's, electron and atomic force microscopy's, and a host of indirect structural methods. A comprehensive understanding of phototransduction requires further structural work on individual components and their relevant complexes in solution and the native disk membrane. Given the accelerated pace of structure determination, it is anticipated that this will be the first G-protein-coupled pathway for which a complete molecular description is ultimately available.

PMID:
13678959
DOI:
10.1016/S0968-0004(03)00172-5
[Indexed for MEDLINE]

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