6fuf: Difference between revisions
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The entry | ==Crystal structure of the rhodopsin-mini-Go complex== | ||
<StructureSection load='6fuf' size='340' side='right' caption='[[6fuf]], [[Resolution|resolution]] 3.12Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fuf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FUF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RHO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN]), GNAO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fuf OCA], [http://pdbe.org/6fuf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fuf RCSB], [http://www.ebi.ac.uk/pdbsum/6fuf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fuf ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/GNAO_HUMAN GNAO_HUMAN]] Early infantile epileptic encephalopathy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/OPSD_BOVIN OPSD_BOVIN]] Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).<ref>PMID:16908857</ref> <ref>PMID:17060607</ref> [[http://www.uniprot.org/uniprot/GNAO_HUMAN GNAO_HUMAN]] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Selective coupling of G protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptors (GPCRs) to specific Galpha-protein subtypes is critical to transform extracellular signals, carried by natural ligands and clinical drugs, into cellular responses. At the center of this transduction event lies the formation of a signaling complex between the receptor and G protein. We report the crystal structure of light-sensitive GPCR rhodopsin bound to an engineered mini-Go protein. The conformation of the receptor is identical to all previous structures of active rhodopsin, including the complex with arrestin. Thus, rhodopsin seems to adopt predominantly one thermodynamically stable active conformation, effectively acting like a "structural switch," allowing for maximum efficiency in the visual system. Furthermore, our analysis of the well-defined GPCR-G protein interface suggests that the precise position of the carboxyl-terminal "hook-like" element of the G protein (its four last residues) relative to the TM7/helix 8 (H8) joint of the receptor is a significant determinant in selective G protein activation. | |||
Crystal structure of rhodopsin in complex with a mini-Go sheds light on the principles of G protein selectivity.,Tsai CJ, Pamula F, Nehme R, Muhle J, Weinert T, Flock T, Nogly P, Edwards PC, Carpenter B, Gruhl T, Ma P, Deupi X, Standfuss J, Tate CG, Schertler GFX Sci Adv. 2018 Sep 19;4(9):eaat7052. doi: 10.1126/sciadv.aat7052. eCollection 2018, Sep. PMID:30255144<ref>PMID:30255144</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6fuf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bovin]] | |||
[[Category: Human]] | |||
[[Category: Carpenter, B]] | |||
[[Category: Deupi, X]] | |||
[[Category: Edwards, P C]] | |||
[[Category: Flock, T]] | |||
[[Category: Gruhl, T]] | |||
[[Category: Ma, P]] | |||
[[Category: Muehle, J]] | |||
[[Category: Nehme, R]] | |||
[[Category: Nogly, P]] | |||
[[Category: Pamula, F]] | |||
[[Category: Schertler, G F.X]] | |||
[[Category: Standfuss, J]] | |||
[[Category: Tate, C G]] | |||
[[Category: Tsai, C J]] | |||
[[Category: Weinert, T]] | |||
[[Category: Gpcr complex rhodopsin]] | |||
[[Category: Signaling protein]] | |||
Latest revision as of 11:38, 10 October 2018
Crystal structure of the rhodopsin-mini-Go complexCrystal structure of the rhodopsin-mini-Go complex
Structural highlights
Disease[GNAO_HUMAN] Early infantile epileptic encephalopathy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function[OPSD_BOVIN] Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).[1] [2] [GNAO_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14. Publication Abstract from PubMedSelective coupling of G protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptors (GPCRs) to specific Galpha-protein subtypes is critical to transform extracellular signals, carried by natural ligands and clinical drugs, into cellular responses. At the center of this transduction event lies the formation of a signaling complex between the receptor and G protein. We report the crystal structure of light-sensitive GPCR rhodopsin bound to an engineered mini-Go protein. The conformation of the receptor is identical to all previous structures of active rhodopsin, including the complex with arrestin. Thus, rhodopsin seems to adopt predominantly one thermodynamically stable active conformation, effectively acting like a "structural switch," allowing for maximum efficiency in the visual system. Furthermore, our analysis of the well-defined GPCR-G protein interface suggests that the precise position of the carboxyl-terminal "hook-like" element of the G protein (its four last residues) relative to the TM7/helix 8 (H8) joint of the receptor is a significant determinant in selective G protein activation. Crystal structure of rhodopsin in complex with a mini-Go sheds light on the principles of G protein selectivity.,Tsai CJ, Pamula F, Nehme R, Muhle J, Weinert T, Flock T, Nogly P, Edwards PC, Carpenter B, Gruhl T, Ma P, Deupi X, Standfuss J, Tate CG, Schertler GFX Sci Adv. 2018 Sep 19;4(9):eaat7052. doi: 10.1126/sciadv.aat7052. eCollection 2018, Sep. PMID:30255144[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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