1iku: Difference between revisions
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==myristoylated recoverin in the calcium-free state, NMR, 22 structures== | ==myristoylated recoverin in the calcium-free state, NMR, 22 structures== | ||
<StructureSection load='1iku' size='340' side='right' caption='[[1iku]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''> | <StructureSection load='1iku' size='340' side='right' caption='[[1iku]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iku]] is a 1 chain structure | <table><tr><td colspan='2'>[[1iku]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IKU FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></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=1iku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iku OCA], [http://pdbe.org/1iku PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iku RCSB], [http://www.ebi.ac.uk/pdbsum/1iku PDBsum]</span></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=1iku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iku OCA], [http://pdbe.org/1iku PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iku RCSB], [http://www.ebi.ac.uk/pdbsum/1iku PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iku ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iku ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ames, J B]] | [[Category: Ames, J B]] | ||
[[Category: Harvey, T S]] | [[Category: Harvey, T S]] | ||
Revision as of 13:41, 27 September 2017
myristoylated recoverin in the calcium-free state, NMR, 22 structuresmyristoylated recoverin in the calcium-free state, NMR, 22 structures
Structural highlights
Function[RECO_BOVIN] Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRecoverin, a retinal calcium-binding protein of relative molecular mass (M(r)) 23K, participates in the recovery phase of visual excitation and in adaptation to background light. The Ca(2+)-bound form of recoverin prolongs the photoresponse, probably by blocking phosphorylation of photoexcited rhodopsin. Retinal recoverin contains a covalently attached myristoyl group or related acyl group at its amino terminus and two Ca(2+)-binding sites. Ca2+ binding to myristoylated, but not unmyristoylated, recoverin induces its translocation to bilayer membranes, indicating that the myristoyl group is essential to the read-out of calcium signals (calcium-myristoyl switch). Here we present the solution structure of Ca(2+)-free, myristoylated recombinant recoverin obtained by heteronuclear multidimensional NMR spectroscopy. The myristoyl group is sequestered in a deep hydrophobic pocket formed by many aromatic and other hydrophobic residues from five flanking helices. Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state.,Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M Nature. 1995 Aug 3;376(6539):444-7. PMID:7630423[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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