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| - | [[Image:1t0h.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1t0h| PDB=1t0h | SCENE= }} | | {{STRUCTURE_1t0h| PDB=1t0h | SCENE= }} |
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| - | '''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=== |
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15141227}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15141227 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15141227}} |
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| | ==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]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:21:07 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:38:03 2008'' |
Revision as of 18:38, 27 July 2008
Template:STRUCTURE 1t0h
Crystal structure of the Rattus norvegicus voltage gated calcium channel beta subunit isoform 2a
Template:ABSTRACT PUBMED 15141227
About this Structure
1T0H is a Protein complex structure of sequences from 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
Page seeded by OCA on Sun Jul 27 21:38:03 2008
