1t0h: Difference between revisions

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[[Image:1t0h.gif|left|200px]]
{{Seed}}
[[Image:1t0h.png|left|200px]]


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{{STRUCTURE_1t0h|  PDB=1t0h  |  SCENE=  }}  
{{STRUCTURE_1t0h|  PDB=1t0h  |  SCENE=  }}  


'''Crystal structure of the Rattus norvegicus voltage gated calcium channel beta subunit isoform 2a'''
===Crystal structure of the Rattus norvegicus voltage gated calcium channel beta subunit isoform 2a===




==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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{{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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