1t0h
From Proteopedia
(New page: 200px<br /><applet load="1t0h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0h, resolution 1.97Å" /> '''Crystal structure of...) |
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| - | [[Image:1t0h.gif|left|200px]]<br /><applet load="1t0h" size=" | + | [[Image:1t0h.gif|left|200px]]<br /><applet load="1t0h" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t0h, resolution 1.97Å" /> | caption="1t0h, resolution 1.97Å" /> | ||
'''Crystal structure of the Rattus norvegicus voltage gated calcium channel beta subunit isoform 2a'''<br /> | '''Crystal structure of the Rattus norvegicus voltage gated calcium channel beta subunit isoform 2a'''<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. |
==About this Structure== | ==About this Structure== | ||
| - | 1T0H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [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:// | + | 1T0H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [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=1T0H 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: nucleotide kinase like domain]] | [[Category: nucleotide kinase like domain]] | ||
[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:30 2008'' |
Revision as of 13:08, 21 February 2008
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Crystal structure of the Rattus norvegicus voltage gated calcium channel beta subunit isoform 2a
Overview
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.
About this Structure
1T0H is a Protein complex structure of sequences from Rattus norvegicus with as ligand. 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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