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| | ==Crystal Structure of the calcium sensor calcium-binding protein 1 (CaBP1)== | | ==Crystal Structure of the calcium sensor calcium-binding protein 1 (CaBP1)== |
| - | <StructureSection load='3ox6' size='340' side='right' caption='[[3ox6]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='3ox6' size='340' side='right'caption='[[3ox6]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ox6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OX6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ox6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OX6 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>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ox5|3ox5]]</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>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</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 Homo sapiens])</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=3ox6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ox6 OCA], [https://pdbe.org/3ox6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ox6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ox6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ox6 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=3ox6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ox6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ox6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ox6 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> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Calcium-binding protein 1 (CaBP1), a calmodulin (CaM) homolog, endows certain voltage-gated calcium channels (Ca(V)s) with unusual properties. CaBP1 inhibits Ca(V)1.2 calcium-dependent inactivation (CDI) and introduces calcium-dependent facilitation (CDF). Here, we show that the ability of CaBP1 to inhibit Ca(V)1.2 CDI and induce CDF arises from interaction between the CaBP1 N-lobe and interlobe linker residue Glu94. Unlike CaM, where functional EF hands are essential for channel modulation, CDI inhibition does not require functional CaBP1 EF hands. Furthermore, CaBP1-mediated CDF has different molecular requirements than CaM-mediated CDF. Overall, the data show that CaBP1 comprises two structural modules having separate functions: similar to CaM, the CaBP1 C-lobe serves as a high-affinity anchor that binds the Ca(V)1.2 IQ domain at a site that overlaps with the Ca(2)+/CaM C-lobe site, whereas the N-lobe/linker module houses the elements required for channel modulation. Discovery of this division provides the framework for understanding how CaBP1 regulates Ca(V)s.
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| - | Structural basis for the differential effects of CaBP1 and calmodulin on Ca(V)1.2 calcium-dependent inactivation.,Findeisen F, Minor DL Jr Structure. 2010 Dec 8;18(12):1617-31. PMID:21134641<ref>PMID:21134641</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Findeisen, F]] | + | [[Category: Large Structures]] |
| - | [[Category: Minor, D L]] | + | [[Category: Findeisen F]] |
| - | [[Category: Calcium binding]] | + | [[Category: Minor DL]] |
| - | [[Category: Calcium binding protein]]
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| - | [[Category: Calcium-sensor]]
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| - | [[Category: Ef-hand]]
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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]
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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