1t0j

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[[Image:1t0j.gif|left|200px]]
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[[Image:1t0j.png|left|200px]]
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{{STRUCTURE_1t0j| PDB=1t0j | SCENE= }}
{{STRUCTURE_1t0j| PDB=1t0j | SCENE= }}
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'''Crystal structure of a complex between voltage-gated calcium channel beta2a subunit and a peptide of the alpha1c subunit'''
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===Crystal structure of a complex between voltage-gated calcium channel beta2a subunit and a peptide of the alpha1c subunit===
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==Overview==
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Voltage-gated calcium channels (Ca(V)s) govern muscle contraction, hormone and neurotransmitter release, neuronal migration, activation of calcium-dependent signalling cascades, and synaptic input integration. An essential Ca(V) intracellular protein, the beta-subunit (Ca(V)beta), binds a conserved domain (the alpha-interaction domain, AID) between transmembrane domains I and II of the pore-forming alpha(1) subunit and profoundly affects multiple channel properties such as voltage-dependent activation, inactivation rates, G-protein modulation, drug sensitivity and cell surface expression. Here, we report the high-resolution crystal structures of the Ca(V)beta2a conserved core, alone and in complex with the AID. Previous work suggested that a conserved region, the beta-interaction domain (BID), formed the AID-binding site; however, this region is largely buried in the Ca(V)beta core and is unavailable for protein-protein interactions. The structure of the AID-Ca(V)beta2a complex shows instead that Ca(V)beta2a engages the AID through an extensive, conserved hydrophobic cleft (named the alpha-binding pocket, ABP). The ABP-AID interaction positions one end of the Ca(V)beta near the intracellular end of a pore-lining segment, called IS6, that has a critical role in Ca(V) inactivation. Together, these data suggest that Ca(V)betas influence Ca(V) gating by direct modulation of IS6 movement within the channel pore.
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The line below this paragraph, {{ABSTRACT_PUBMED_15141227}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15141227 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15141227}}
==About this Structure==
==About this Structure==
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[[Category: Nucleotide kinase like domain]]
[[Category: Nucleotide kinase like domain]]
[[Category: Sh3 domain]]
[[Category: Sh3 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:21:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:33:45 2008''

Revision as of 11:33, 27 July 2008

Image:1t0j.png

Template:STRUCTURE 1t0j

Crystal structure of a complex between voltage-gated calcium channel beta2a subunit and a peptide of the alpha1c subunit

Template:ABSTRACT PUBMED 15141227

About this Structure

1T0J is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain., Van Petegem F, Clark KA, Chatelain FC, Minor DL Jr, Nature. 2004 Jun 10;429(6992):671-5. Epub 2004 May 12. PMID:15141227

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