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| | ==NMR Structure of Ca2+-bound CaBP1 C-domain== | | ==NMR Structure of Ca2+-bound CaBP1 C-domain== |
| - | <StructureSection load='2k7d' size='340' side='right' caption='[[2k7d]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='2k7d' size='340' side='right'caption='[[2k7d]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2k7d]] 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=2K7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K7D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2k7d]] 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=2K7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K7D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k7b|2k7b]], [[2k7c|2k7c]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CABP1 ([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=2k7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7d OCA], [https://pdbe.org/2k7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k7d RCSB], [https://www.ebi.ac.uk/pdbsum/2k7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7d ProSAT]</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=2k7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7d OCA], [http://pdbe.org/2k7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k7d RCSB], [http://www.ebi.ac.uk/pdbsum/2k7d PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CABP1_HUMAN CABP1_HUMAN]] Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but resulting in an opposit effects on channel function. Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration (By similarity).<ref>PMID:11865310</ref> <ref>PMID:14570872</ref> <ref>PMID:15140941</ref> <ref>PMID:15980432</ref> <ref>PMID:15895247</ref> | + | [https://www.uniprot.org/uniprot/CABP1_HUMAN CABP1_HUMAN] Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but resulting in an opposit effects on channel function. Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration (By similarity).<ref>PMID:11865310</ref> <ref>PMID:14570872</ref> <ref>PMID:15140941</ref> <ref>PMID:15980432</ref> <ref>PMID:15895247</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/2k7d_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/2k7d_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Ames, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Cabp1]] | + | [[Category: Ames J]] |
| - | [[Category: Cell membrane]]
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| - | [[Category: Cytoskeleton]]
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| - | [[Category: Ef-hand]]
| + | |
| - | [[Category: Ip3 receptor]]
| + | |
| - | [[Category: Lipoprotein]]
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| - | [[Category: Membrane]]
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| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Myristate]]
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| Structural highlights
Function
CABP1_HUMAN Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but resulting in an opposit effects on channel function. Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration (By similarity).[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Lee A, Westenbroek RE, Haeseleer F, Palczewski K, Scheuer T, Catterall WA. Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1. Nat Neurosci. 2002 Mar;5(3):210-7. PMID:11865310 doi:10.1038/nn805
- ↑ Haynes LP, Tepikin AV, Burgoyne RD. Calcium-binding protein 1 is an inhibitor of agonist-evoked, inositol 1,4,5-trisphosphate-mediated calcium signaling. J Biol Chem. 2004 Jan 2;279(1):547-55. Epub 2003 Oct 21. PMID:14570872 doi:10.1074/jbc.M309617200
- ↑ Zhou H, Kim SA, Kirk EA, Tippens AL, Sun H, Haeseleer F, Lee A. Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels. J Neurosci. 2004 May 12;24(19):4698-708. PMID:15140941 doi:10.1523/JNEUROSCI.5523-03.2004
- ↑ Zhou H, Yu K, McCoy KL, Lee A. Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1. J Biol Chem. 2005 Aug 19;280(33):29612-9. Epub 2005 Jun 26. PMID:15980432 doi:M504167200
- ↑ Kinoshita-Kawada M, Tang J, Xiao R, Kaneko S, Foskett JK, Zhu MX. Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus oocytes. Pflugers Arch. 2005 Aug;450(5):345-54. Epub 2005 May 14. PMID:15895247 doi:10.1007/s00424-005-1419-1
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