2001
DOI: 10.1152/physrev.2001.81.4.1659
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Rhodopsin: Structural Basis of Molecular Physiology

Abstract: The crystal structure of rod cell visual pigment rhodopsin was recently solved at 2.8-A resolution. A critical evaluation of a decade of structure-function studies is now possible. It is also possible to begin to explain the structural basis for several unique physiological properties of the vertebrate visual system, including extremely low dark noise levels as well as high gain and color detection. The ligand-binding pocket of rhodopsin is remarkably compact, and several apparent chromophore-protein interacti… Show more

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Cited by 297 publications
(309 citation statements)
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References 255 publications
(217 reference statements)
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“…The CarO protein belongs to the opsin family and was found to show significant degrees of identity with ops and nop-1 from Leptospaeria maculans and Neurospora crassa, respectively. Opsins are membrane photoreceptors which play an important role in light detection in algae (Ridge 2002) and animals (Menon et al 2001). However, understanding the biological function of these proteins in fungi needs further investigations.…”
Section: Discussionmentioning
confidence: 99%
“…The CarO protein belongs to the opsin family and was found to show significant degrees of identity with ops and nop-1 from Leptospaeria maculans and Neurospora crassa, respectively. Opsins are membrane photoreceptors which play an important role in light detection in algae (Ridge 2002) and animals (Menon et al 2001). However, understanding the biological function of these proteins in fungi needs further investigations.…”
Section: Discussionmentioning
confidence: 99%
“…Several highly conserved motifs in GPCRs are also present in the MOR42 subfamily, including the (D/E)R(Y/W) motif located near the cytoplasmic end of TMIII and the NPXXY motif in TMVII. These motifs are thought to form a hydrogen bond network important for inter-helical interactions (37) and may play a role in receptor transformation from an inactive form to an active, G protein-coupled conformation (38). Conserved prolines that produce kinks in the helix structure of MOR42-3 are Pro-162 (in TMIV, equivalent to Pro-170 in rhodopsin) and Pro-303 (in TMVII, position 291 in rhodopsin).…”
Section: Initial Mutation Screen Of Mor42-3-mentioning
confidence: 99%
“…Kozmik et al 2008;Menon et al 2001;Salcedo et al 2003;Yokoyama 1997). In addition, several studies have investigated the molecular basis of the multiple steps in phototransduction, from opsin activation to nervous impulse.…”
Section: Origins Of Variation In Eye Evolutionmentioning
confidence: 99%