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CONSTITUTIVELY ACTIVE MUTANTS OF RHODOPSIN
Author(s): ROBINSON PR, COHEN GB, ZHUKOVSKY EA, OPRIAN DD
Source: NEURON    Volume: 9    Issue: 4    Pages: 719-725    Published: OCT 1992  
Times Cited: 368     References: 42     
Abstract: Two critical amino acids in the visual pigment rhodopsin are Lys-296, the site of attachment of retinal to the protein through a protonated Schiff base linkage, and Glu-113, the Schiff base counterion. Mutation of Lys-296 or Glu-113 results in constitutive activation of opsin, as assayed by its ability to activate transducin in the absence of added chromophore. We conclude that opsin is constrained to an inactive conformation by a salt bridge between Lys-296 and Glu-113. Recently, one of the mutants, K296E, was found in a family with retinitis pigmentosa, suggesting that degeneration of the photoreceptor cells in individuals with this mutation may result from persistent stimulation of the phototransduction pathway.
Document Type: Article
Language: English
Reprint Address: ROBINSON, PR (reprint author), BRANDEIS UNIV, GRAD DEPT BIOCHEM, WALTHAM, MA 02254 USA
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138
Subject Category: Neurosciences
IDS Number: JT516
ISSN: 0896-6273
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