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    J Struct Biol. 2011 Dec;176(3):387-94. Epub 2011 Sep 6.

    Rhodopsin-transducin heteropentamer: three-dimensional structure and biochemical characterization.

    Source

    Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106-4965, USA. bxj27@case.edu

    Abstract

    The process of vision is initiated when the G protein-coupled receptor, rhodopsin (Rho), absorbs a photon and transitions to its activated Rho(∗) form. Rho(∗) binds the heterotrimeric G protein, transducin (G(t)) inducing GDP to GTP exchange and G(t) dissociation. Using nucleotide depletion and affinity chromatography, we trapped and purified the resulting nucleotide-free Rho(∗)·G(t) complex. Quantitative SDS-PAGE suggested a 2:1 molar ratio of Rho(∗) to G(t) in the complex and its mass determined by scanning transmission electron microscopy was 221±12kDa. A 21.6Å structure was calculated from projections of negatively stained Rho(∗)·G(t) complexes. The molecular envelope thus determined accommodated two Rho molecules together with one G(t) heterotrimer, corroborating the heteropentameric structure of the Rho(∗)·G(t) complex.

    Copyright © 2011 Elsevier Inc. All rights reserved.

    PMID:
    21925606
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC3210324
    [Available on 2012/12/1]

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