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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 [http://en.wikipedia.org/wiki/Human Human]. 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> |
| | </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='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> |
| | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ox5|3ox5]]</td></tr> | | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ox5|3ox5]]</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='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'>[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> | + | <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://pdbe.org/3ox6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ox6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ox6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ox6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3ox6" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Homo sapiens]] | + | [[Category: Human]] |
| | [[Category: Findeisen, F]] | | [[Category: Findeisen, F]] |
| | [[Category: Minor, D L]] | | [[Category: Minor, D L]] |
| 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]
Publication Abstract from PubMed
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.
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[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Findeisen F, Minor DL Jr. Structural basis for the differential effects of CaBP1 and calmodulin on Ca(V)1.2 calcium-dependent inactivation. Structure. 2010 Dec 8;18(12):1617-31. PMID:21134641 doi:10.1016/j.str.2010.09.012
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