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1iku

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Revision as of 07:44, 7 April 2021

myristoylated recoverin in the calcium-free state, NMR, 22 structures

Structural highlights

1iku is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Recoverin, 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.

References

↑ Hurley JB, Dizhoor AM, Ray S, Stryer L. Recoverin's role: conclusion withdrawn. Science. 1993 May 7;260(5109):740. PMID:8097896
↑ Kawamura S, Hisatomi O, Kayada S, Tokunaga F, Kuo CH. Recoverin has S-modulin activity in frog rods. J Biol Chem. 1993 Jul 15;268(20):14579-82. PMID:8392055
↑ Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M. Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature. 1995 Aug 3;376(6539):444-7. PMID:7630423 doi:http://dx.doi.org/10.1038/376444a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iku"

@@ Line 3: / Line 3: @@
 <StructureSection load='1iku' size='340' side='right'caption='[[1iku]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
 == Structural highlights ==
-<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>
+<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 [https://proteopedia.org/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" id="ligandDat"><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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iku ProSAT]</span></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=1iku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iku OCA], [https://pdbe.org/1iku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iku RCSB], [https://www.ebi.ac.uk/pdbsum/1iku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iku ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RECO_BOVIN 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.<ref>PMID:8097896</ref> <ref>PMID:8392055</ref>
+[[https://www.uniprot.org/uniprot/RECO_BOVIN 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.<ref>PMID:8097896</ref> <ref>PMID:8392055</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1iku

From Proteopedia

Revision as of 07:44, 7 April 2021

myristoylated recoverin in the calcium-free state, NMR, 22 structures

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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