1T3S

Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core

1T3S の概要

• エントリーDOI: 10.2210/pdb1t3s/pdb
• 関連するPDBエントリー: 1T3L
• 分子名称: Dihydropyridine-sensitive L-type, calcium channel beta-2 subunit, MERCURY (II) ION (3 entities in total)
• 機能のキーワード: sh3 domain, guanylate kinase domain, transport protein
• 由来する生物種: Oryctolagus cuniculus (rabbit); 詳細
• 細胞内の位置: Cell membrane, sarcolemma ; Peripheral membrane protein ; Cytoplasmic side : P54288
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38541.54

構造登録者

Opatowsky, Y.,Chen, C.-C.,Campbell, K.P.,Hirsch, J.A. (登録日: 2004-04-27, 公開日: 2004-05-25, 最終更新日: 2024-04-03)

主引用文献

Opatowsky, Y.,Chen, C.C.,Campbell, K.P.,Hirsch, J.A.
Structural analysis of the voltage-dependent calcium channel beta subunit functional core and its complex with the alpha 1 interaction domain.
Neuron, 42:387-399, 2004

PubMed Abstract: Voltage-dependent calcium channels (VDCC) are multiprotein assemblies that regulate the entry of extracellular calcium into electrically excitable cells and serve as signal transduction centers. The alpha1 subunit forms the membrane pore while the intracellular beta subunit is responsible for trafficking of the channel to the plasma membrane and modulation of its electrophysiological properties. Crystallographic analyses of a beta subunit functional core alone and in complex with a alpha1 interaction domain (AID) peptide, the primary binding site of beta to the alpha1 subunit, reveal that beta represents a novel member of the MAGUK protein family. The findings illustrate how the guanylate kinase fold has been fashioned into a protein-protein interaction module by alteration of one of its substrate sites. Combined results indicate that the AID peptide undergoes a helical transition in binding to beta. We outline the mechanistic implications for understanding the beta subunit's broad regulatory role of the VDCC, particularly via the AID.

PubMed: 15134636
DOI: 10.1093/hmg/ddh162

実験手法

X-RAY DIFFRACTION (2.3 Å)