1vyv
From Proteopedia
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| - | [[Image:1vyv.jpg|left|200px]] | + | [[Image:1vyv.jpg|left|200px]] |
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| - | '''BETA4 SUBUNIT OF CA2+ CHANNEL''' | + | {{Structure |
| + | |PDB= 1vyv |SIZE=350|CAPTION= <scene name='initialview01'>1vyv</scene>, resolution 3.Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''BETA4 SUBUNIT OF CA2+ CHANNEL''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VYV is a [ | + | 1VYV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYV OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels., Chen YH, Li MH, Zhang Y, He LL, Yamada Y, Fitzmaurice A, Shen Y, Zhang H, Tong L, Yang J, Nature. 2004 Jun 10;429(6992):675-80. Epub 2004 May 30. PMID:[http:// | + | Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels., Chen YH, Li MH, Zhang Y, He LL, Yamada Y, Fitzmaurice A, Shen Y, Zhang H, Tong L, Yang J, Nature. 2004 Jun 10;429(6992):675-80. Epub 2004 May 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15170217 15170217] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: voltage-gated channel]] | [[Category: voltage-gated channel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:49:52 2008'' |
Revision as of 12:49, 20 March 2008
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BETA4 SUBUNIT OF CA2+ CHANNEL
Overview
High-voltage-activated Ca2+ channels are essential for diverse biological processes. They are composed of four or five subunits, including alpha1, alpha2-delta, beta and gamma (ref. 1). Their expression and function are critically dependent on the beta-subunit, which transports alpha1 to the surface membrane and regulates diverse channel properties. It is believed that the beta-subunit interacts with alpha1 primarily through the beta-interaction domain (BID), which binds directly to the alpha-interaction domain (AID) of alpha1; however, the molecular mechanism of the alpha1-beta interaction is largely unclear. Here we report the crystal structures of the conserved core region of beta3, alone and in complex with AID, and of beta4 alone. The structures show that the beta-subunit core contains two interacting domains: a Src homology 3 (SH3) domain and a guanylate kinase (GK) domain. The AID binds to a hydrophobic groove in the GK domain through extensive interactions, conferring extremely high affinity between alpha1 and beta-subunits. The BID is essential both for the structural integrity of and for bridging the SH3 and GK domains, but it does not participate directly in binding alpha1. The presence of multiple protein-interacting modules in the beta-subunit opens a new dimension to its function as a multi-functional protein.
About this Structure
1VYV is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels., Chen YH, Li MH, Zhang Y, He LL, Yamada Y, Fitzmaurice A, Shen Y, Zhang H, Tong L, Yang J, Nature. 2004 Jun 10;429(6992):675-80. Epub 2004 May 30. PMID:15170217
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