4DEX

Crystal structure of the Voltage Dependent Calcium Channel beta-2 Subunit in Complex With The CaV2.2 I-II Linker.

4DEX の概要

• エントリーDOI: 10.2210/pdb4dex/pdb
• 関連するPDBエントリー: 1t3l 4DEY
• 分子名称: Voltage-dependent L-type calcium channel subunit beta-2, Voltage-dependent N-type calcium channel subunit alpha-1B (3 entities in total)
• 機能のキーワード: maguk, voltage dependent calcium channel, transport protein
• 由来する生物種: Oryctolagus cuniculus (European rabbit,Japanese white rabbit,domestic rabbit,rabbits); 詳細
• 細胞内の位置: Cell membrane, sarcolemma ; Peripheral membrane protein ; Cytoplasmic side : P54288; Membrane; Multi-pass membrane protein: Q02294
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51543.75

構造登録者

Almagor, L.,Hirsch, J.A. (登録日: 2012-01-22, 公開日: 2012-06-13, 最終更新日: 2024-02-28)

主引用文献

Almagor, L.,Chomsky-Hecht, O.,Ben-Mocha, A.,Hendin-Barak, D.,Dascal, N.,Hirsch, J.A.
The role of a voltage-dependent Ca2+ channel intracellular linker: a structure-function analysis.
J.Neurosci., 32:7602-7613, 2012

PubMed Abstract: Voltage-dependent calcium channels (VDCCs) allow the passage of Ca(2+) ions through cellular membranes in response to membrane depolarization. The channel pore-forming subunit, α1, and a regulatory subunit (Ca(V)β) form a high affinity complex where Ca(V)β binds to a α1 interacting domain in the intracellular linker between α1 membrane domains I and II (I-II linker). We determined crystal structures of Ca(V)β2 functional core in complex with the Ca(V)1.2 and Ca(V)2.2 I-II linkers to a resolution of 1.95 and 2.0 Å, respectively. Structural differences between the highly conserved linkers, important for coupling Ca(V)β to the channel pore, guided mechanistic functional studies. Electrophysiological measurements point to the importance of differing linker structure in both Ca(V)1 and 2 subtypes with mutations affecting both voltage- and calcium-dependent inactivation and voltage dependence of activation. These linker effects persist in the absence of Ca(V)β, pointing to the intrinsic role of the linker in VDCC function and suggesting that I-II linker structure can serve as a brake during inactivation.

PubMed: 22649239
DOI: 10.1523/JNEUROSCI.5727-11.2012

実験手法

X-RAY DIFFRACTION (2 Å)