Crystal structure of squid rhodopsin

  title={Crystal structure of squid rhodopsin},
  author={Midori Murakami and Tsutomu Kouyama},
Invertebrate phototransduction uses an inositol-1,4,5-trisphosphate signalling cascade in which photoactivated rhodopsin stimulates a Gq-type G protein, that is, a class of G protein that stimulates membrane-bound phospholipase Cβ. The same cascade is used by many G-protein-coupled receptors, indicating that invertebrate rhodopsin is a prototypical member. Here we report the crystal structure of squid (Todarodes pacificus) rhodopsin at 2.5 Å resolution. Among seven transmembrane α-helices… 

Crystallographic analysis of the primary photochemical reaction of squid rhodopsin.

Dynamics of the internal water molecules in squid rhodopsin.

A G protein-coupled receptor at work: the rhodopsin model.

Comparative Analysis of GPCR Crystal Structures †

To fully understand the structural and functional aspects of rhodopsin it is necessary to critically examine crystal structures of its different photointermediates.

Recent advances in biophysical studies of rhodopsins - Oligomerization, folding, and structure.

  • L. BrownO. Ernst
  • Biology, Chemistry
    Biochimica et biophysica acta. Proteins and proteomics
  • 2017

Structural divergence and functional versatility of the rhodopsin superfamily.

  • T. KouyamaM. Murakami
  • Biology
    Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
  • 2010
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Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structural

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Preliminary crystallographic analysis, together with linear dichroism results, suggested that the rhodopsin dimers are packed in such a manner that their transmembrane helices are aligned nearly parallel to the c axis.

Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane.

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High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor.

Although the location of carazolol in the beta2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopin as a template model for this large receptor family.

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High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor

Although the location of carazolol in the β2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopin as a template model for this large receptor family.

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