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1VYU

Beta3 subunit of Voltage-gated Ca2+-channel

1VYU の概要
エントリーDOI10.2210/pdb1vyu/pdb
関連するPDBエントリー1VYT 1VYV
分子名称CALCIUM CHANNEL BETA-3 SUBUNIT (2 entities in total)
機能のキーワードcalcium channel beta subunit, aid doamin, ion transport, ionic channel, voltage-gated channel, sh3 domain
由来する生物種RATTUS NORVEGICUS (RAT)
タンパク質・核酸の鎖数2
化学式量合計79552.52
構造登録者
Chen, Y.-H.,Li, M.-H.,Zhang, Y.,He, L.-L.,Yamada, Y.,Fitzmaurice, A.,Yang, S.,Zhang, H.,Liang, T.,Yang, J. (登録日: 2004-05-07, 公開日: 2004-06-15, 最終更新日: 2024-11-06)
主引用文献Chen, Y.-H.,Li, M.-H.,Zhang, Y.,He, L.-L.,Yamada, Y.,Fitzmaurice, A.,Shen, Y.,Zhang, H.,Tong, L.,Yang, J.
Structural Basis of the Alpha(1)-Beta Subunit Interaction of Voltage-Gated Ca(2+) Channels
Nature, 429:675-, 2004
Cited by
PubMed Abstract: 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.
PubMed: 15170217
DOI: 10.1038/NATURE02641
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.3 Å)
構造検証レポート
Validation report summary of 1vyu
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-20に公開中

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