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| | ==NMR STRUCTURE OF THE RHODOPSIN-BOUND C-TERMINAL PEPTIDE OF THE TRANSDUCIN ALPHA-SUBUNIT, 20 STRUCTURES== | | ==NMR STRUCTURE OF THE RHODOPSIN-BOUND C-TERMINAL PEPTIDE OF THE TRANSDUCIN ALPHA-SUBUNIT, 20 STRUCTURES== |
| - | <StructureSection load='1aqg' size='340' side='right'caption='[[1aqg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1aqg' size='340' side='right'caption='[[1aqg]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1aqg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AQG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1aqg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AQG FirstGlance]. <br> |
| - | </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=1aqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aqg OCA], [http://pdbe.org/1aqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aqg RCSB], [http://www.ebi.ac.uk/pdbsum/1aqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aqg ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aqg OCA], [https://pdbe.org/1aqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aqg RCSB], [https://www.ebi.ac.uk/pdbsum/1aqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aqg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GNAT1_BOVIN GNAT1_BOVIN]] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase. | + | [https://www.uniprot.org/uniprot/GNAT1_BOVIN GNAT1_BOVIN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kisselev, O G]] | + | [[Category: Kisselev OG]] |
| - | [[Category: Marshall, G R]] | + | [[Category: Marshall GR]] |
| - | [[Category: Gtp-binding]]
| + | |
| - | [[Category: Rhodopsin]]
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| - | [[Category: Transducer]]
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| - | [[Category: Transducin]]
| + | |
| Structural highlights
Function
GNAT1_BOVIN Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.
Publication Abstract from PubMed
A large superfamily of transmembrane receptors control cellular responses to diverse extracellular signals by catalyzing activation of specific types of heterotrimeric GTP-binding proteins. How these receptors recognize and promote nucleotide exchange on G protein alpha subunits to initiate signal amplification is unknown. The three-dimensional structure of the transducin (Gt) alpha subunit C-terminal undecapeptide Gtalpha(340-350) IKENLKDCGLF was determined by transferred nuclear Overhauser effect spectroscopy while it was bound to photoexcited rhodopsin. Light activation of rhodopsin causes a dramatic shift from a disordered conformation of Gtalpha(340-350) to a binding motif with a helical turn followed by an open reverse turn centered at Gly-348, a helix-terminating C capping motif of an alphaL type. Docking of the NMR structure to the GDP-bound x-ray structure of Gt reveals that photoexcited rhodopsin promotes the formation of a continuous helix over residues 325-346 terminated by the C-terminal helical cap with a unique cluster of crucial hydrophobic side chains. A molecular mechanism by which activated receptors can control G proteins through reversible conformational changes at the receptor-G protein interface is demonstrated.
Light-activated rhodopsin induces structural binding motif in G protein alpha subunit.,Kisselev OG, Kao J, Ponder JW, Fann YC, Gautam N, Marshall GR Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4270-5. PMID:9539726[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kisselev OG, Kao J, Ponder JW, Fann YC, Gautam N, Marshall GR. Light-activated rhodopsin induces structural binding motif in G protein alpha subunit. Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4270-5. PMID:9539726
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