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| | ==Solution structure of calcium free, myristoylated visinin-like protein 3== | | ==Solution structure of calcium free, myristoylated visinin-like protein 3== |
| - | <StructureSection load='5t7c' size='340' side='right'caption='[[5t7c]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='5t7c' size='340' side='right'caption='[[5t7c]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5t7c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T7C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5T7C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5t7c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T7C FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HPCAL1, BDR1 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5t7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t7c OCA], [https://pdbe.org/5t7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t7c RCSB], [https://www.ebi.ac.uk/pdbsum/5t7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t7c ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5t7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t7c OCA], [http://pdbe.org/5t7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t7c RCSB], [http://www.ebi.ac.uk/pdbsum/5t7c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t7c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HPCL1_HUMAN HPCL1_HUMAN]] May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. | + | [https://www.uniprot.org/uniprot/HPCL1_HUMAN HPCL1_HUMAN] May be involved in the calcium-dependent regulation of rhodopsin phosphorylation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ames, J B]] | + | [[Category: Ames JB]] |
| - | [[Category: Lim, S]] | + | [[Category: Lim S]] |
| - | [[Category: Calmodulin]]
| + | |
| - | [[Category: Hippocalcin]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Neuronal calcium sensor]]
| + | |
| Structural highlights
Function
HPCL1_HUMAN May be involved in the calcium-dependent regulation of rhodopsin phosphorylation.
Publication Abstract from PubMed
Visinin-like protein 3 (VILIP-3) belongs to a family of Ca2+-myristoyl switch proteins that regulate signal transduction in the brain and retina. Here we analyze Ca2+ binding, characterize Ca2+-induced conformational changes, and determine the NMR structure of myristoylated VILIP-3. Three Ca2+ bind cooperatively to VILIP-3 at EF2, EF3 and EF4 (KD = 0.52 muM and Hill slope of 1.8). NMR assignments, mutagenesis and structural analysis indicate that the covalently attached myristoyl group is solvent exposed in Ca2+-bound VILIP-3, whereas Ca2+-free VILIP-3 contains a sequestered myristoyl group that interacts with protein residues (E26, Y64, V68), which are distinct from myristate contacts seen in other Ca2+-myristoyl switch proteins. The myristoyl group in VILIP-3 forms an unusual L-shaped structure that places the C14 methyl group inside a shallow protein groove, in contrast to the much deeper myristoyl binding pockets observed for recoverin, NCS-1 and GCAP1. Thus, the myristoylated VILIP-3 protein structure determined in this study is quite different from those of other known myristoyl switch proteins (recoverin, NCS-1, and GCAP1). We propose that myristoylation serves to fine tune the three-dimensional structures of neuronal calcium sensor proteins as a means of generating functional diversity.
Structure and Calcium Binding Properties of a Neuronal Calcium-Myristoyl Switch Protein, Visinin-Like Protein 3.,Li C, Lim S, Braunewell KH, Ames JB PLoS One. 2016 Nov 7;11(11):e0165921. doi: 10.1371/journal.pone.0165921., eCollection 2016. PMID:27820860[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li C, Lim S, Braunewell KH, Ames JB. Structure and Calcium Binding Properties of a Neuronal Calcium-Myristoyl Switch Protein, Visinin-Like Protein 3. PLoS One. 2016 Nov 7;11(11):e0165921. doi: 10.1371/journal.pone.0165921., eCollection 2016. PMID:27820860 doi:http://dx.doi.org/10.1371/journal.pone.0165921
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