Solution structure of the N-terminal A domain of the human voltage-gated Ca2+channel beta4a subunit.
Solution structure of the N-terminal A domain of the human voltage-gated Ca2+channel beta4a subunit.
复制标题
人类电压门控 Ca2 通道 beta4a 亚基 N 端 A 结构域的溶液结构。
DOI:
10.1110/ps.051894506
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发表时间:
2006
期刊:
影响因子:
--
通讯作者:
Horne,WilliamA
中科院分区:
文献类型:
--
作者:
Vendel,AndrewC;Rithner,ChristopherD;Lyons,BarbaraA;Horne,WilliamA
Ca2+channel β subunits regulate trafficking and gating (opening and closing) of voltage‐dependent Ca2+channel α1subunits. Based on primary sequence comparisons, they are thought to be modular structures composed of five domains (A–E) that are related to the large family of membrane associated guanylate‐kinase (MAGUK) proteins. The crystal structures of the β subunit core, B–D, domains have recently been reported; however, very little is known about the structures of the A and E domains. The N‐terminal A domain is a hypervariable region that differs among the four subtypes of Ca2+channel β subunits (β1–β4). Furthermore, this domain undergoes alternative splicing to create multiple N‐terminal structures within a given gene class that have distinct effects on gating. We have solved the solution structure of the A domain of the human β4asubunit, a splice variant that we have shown previously to have α1subunit subtype‐specific effects on Ca2+channel trafficking and gating.