1t0j: Difference between revisions
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New page: left|200px<br /> <applet load="1t0j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0j, resolution 2.00Å" /> '''Crystal structure o... |
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[[Image:1t0j.gif|left|200px]]<br /> | [[Image:1t0j.gif|left|200px]]<br /><applet load="1t0j" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1t0j" size=" | |||
caption="1t0j, resolution 2.00Å" /> | caption="1t0j, resolution 2.00Å" /> | ||
'''Crystal structure of a complex between voltage-gated calcium channel beta2a subunit and a peptide of the alpha1c subunit'''<br /> | '''Crystal structure of a complex between voltage-gated calcium channel beta2a subunit and a peptide of the alpha1c subunit'''<br /> | ||
==Overview== | ==Overview== | ||
Voltage-gated calcium channels (Ca(V)s) govern muscle contraction, hormone | 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. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1T0J is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1T0J is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0J OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Chatelain, F.]] | [[Category: Chatelain, F.]] | ||
[[Category: Clark, K.]] | [[Category: Clark, K.]] | ||
[[Category: Jr., D | [[Category: Jr., D Minor.]] | ||
[[Category: Petegem, F | [[Category: Petegem, F Van.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: aid]] | [[Category: aid]] | ||
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[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:35 2008'' | ||
