来自牛心肌的II型环磷酸腺苷依赖性蛋白激酶调节亚基的一级结构。
Primary structure of the regulatory subunit of type II cAMP-dependent protein kinase from bovine cardiac muscle.
作者信息
Takio K, Smith S B, Krebs E G, Walsh K A, Titani K
出版信息
Proc Natl Acad Sci U S A. 1982 Apr;79(8):2544-8. doi: 10.1073/pnas.79.8.2544.
Abstract
The complete amino acid sequence of the regulatory subunit of type II cAMP-dependent protein kinase from bovine cardiac muscle is presented. Primary fragments for the sequence determination were obtained by limited proteolysis with various proteases or by cleavage with cyanogen bromide. The sequence of the 400 amino acid residues has two homologous regions, strongly suggesting tandem gene duplication. The predicted secondary structure suggests the presence of 42% alpha-helix, 23% beta-strand, and 23 beta-turns. The molecular weight of the subunit, as derived from the sequence, is 45,084 including a phosphate group at residue 95. This is significantly less than earlier estimates based on NaDodSO4 gel electrophoresis and sedimentation experiments. The structure is discussed in terms of putative sites of interaction with cAMP and with the catalytic subunit.
摘要
本文给出了牛心肌II型环磷酸腺苷（cAMP）依赖性蛋白激酶调节亚基的完整氨基酸序列。用于序列测定的初级片段通过用各种蛋白酶进行有限的蛋白水解或用溴化氰裂解获得。400个氨基酸残基的序列有两个同源区域，强烈暗示串联基因重复。预测的二级结构表明存在42%的α-螺旋、23%的β-链和23%的β-转角。根据序列推导，该亚基的分子量为45,084，包括第95位残基处的一个磷酸基团。这明显低于早期基于十二烷基硫酸钠（NaDodSO4）凝胶电泳和沉降实验的估计值。从与cAMP和催化亚基相互作用的假定位点方面对该结构进行了讨论。
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