α1‐β interaction in voltage‐gated cardiac L‐type calcium channels

FEBS Letters

Flockerzi, Veit¹  Marquart, Andrea¹ 

[1]Institut für Pharmakologie, Universität Heidelberg, Im Neuenheimer Feld 366, D-69120 Heidelberg, Germany

关键词: High-voltage-gated calcium channel;    Subunit composition;    Protein interaction;    Epitope library;    Protein probing;    aa;    amino acids;    DNase I;    deoxyribonuclease I;    PBS;    phosphate-buffered saline;    PMSF;    phenylmethylsulfonyl fluoride;    SDS;    sodium dodecylsulfate;   

DOI  :  10.1016/S0014-5793(97)00316-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The β subunits of voltage-gated calcium channels normalize current amplitude, kinetics and voltage dependence of these channels by interacting with the channel's pore forming subunit α₁. By screening an epitope expression library of α_1Ca fusion proteins, a β2a binding site of 22 amino acids was identified within the I–II cytoplasmic linker but not on other cytoplasmic sequences of α_1Ca. This binding site overlaps by 14 amino acids with the conserved 18 amino acid peptide assumed to be essential for α₁-β interaction. The common 14 amino acid motif of α_1Ca is sufficient to bind β2a, and in addition β1a, β3 and β4.

【 授权许可】

Unknown