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5v2p

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==CaV beta2a subunit: CaV1.2 AID-CAP complex==
==CaV beta2a subunit: CaV1.2 AID-CAP complex==
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<StructureSection load='5v2p' size='340' side='right' caption='[[5v2p]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='5v2p' size='340' side='right'caption='[[5v2p]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5v2p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V2P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5v2p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V2P FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=8VY:1,3-bis(bromomethyl)benzene'>8VY</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v2q|5v2q]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=8VY:1,3-bis(bromomethyl)benzene'>8VY</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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<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=5v2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v2p OCA], [http://pdbe.org/5v2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v2p RCSB], [http://www.ebi.ac.uk/pdbsum/5v2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v2p ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5v2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v2p OCA], [https://pdbe.org/5v2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v2p RCSB], [https://www.ebi.ac.uk/pdbsum/5v2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v2p ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[http://www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Defects in CACNA1C are the cause of Timothy syndrome (TS) [MIM:[http://omim.org/entry/601005 601005]]. TS is a disorder characterized by multiorgan dysfunction including lethal arrhythmias, webbing of fingers and toes, congenital heart disease, immune deficiency, intermittent hypoglycemia, cognitive abnormalities and autism.<ref>PMID:15454078</ref> <ref>PMID:15863612</ref> Defects in CACNA1C are the cause of Brugada syndrome type 3 (BRGDA3) [MIM:[http://omim.org/entry/611875 611875]]. A heart disease characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome is a tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs (called ventricular fibrillation), the individual will faint and may die in a few minutes if the heart is not reset.<ref>PMID:17224476</ref>
 
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CACB2_RAT CACB2_RAT]] The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting (By similarity).<ref>PMID:1370480</ref> <ref>PMID:11604404</ref> <ref>PMID:12042350</ref> [[http://www.uniprot.org/uniprot/CAC1C_HUMAN CAC1C_HUMAN]] Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function.<ref>PMID:8392192</ref> <ref>PMID:7737988</ref> <ref>PMID:9013606</ref> <ref>PMID:9607315</ref> <ref>PMID:12176756</ref> <ref>PMID:17071743</ref>
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[https://www.uniprot.org/uniprot/CACB2_RAT CACB2_RAT] The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting (By similarity).<ref>PMID:1370480</ref> <ref>PMID:11604404</ref> <ref>PMID:12042350</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5v2p" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5v2p" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Ion channels 3D structures|Ion channels 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Campiglio, M]]
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[[Category: Homo sapiens]]
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[[Category: Degrado, W F]]
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[[Category: Large Structures]]
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[[Category: Findeisen, F]]
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[[Category: Rattus norvegicus]]
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[[Category: Flucher, B]]
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[[Category: Campiglio M]]
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[[Category: Jo, H]]
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[[Category: Degrado WF]]
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[[Category: Minor, D L]]
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[[Category: Findeisen F]]
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[[Category: Pope, L]]
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[[Category: Flucher B]]
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[[Category: Rumpf, C H]]
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[[Category: Jo H]]
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[[Category: Calcium]]
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[[Category: Minor DL]]
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[[Category: Ion channel]]
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[[Category: Pope L]]
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[[Category: Signaling]]
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[[Category: Rumpf CH]]
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[[Category: Transport protein]]
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Current revision

CaV beta2a subunit: CaV1.2 AID-CAP complex

PDB ID 5v2p

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