Amino acid sequence of rabbit skeletal muscle myosin light chain kinase.
Amino acid sequence of rabbit skeletal muscle myosin light chain kinase.
复制标题
兔骨骼肌肌球蛋白轻链激酶的氨基酸序列。
作者：
K. Takio;D. Blumenthal;K. Walsh;K. Titani;E. Krebs
测定了兔骨骼肌肌球蛋白轻链激酶氨基端235个氨基酸的序列。与先前描述的羧基末端区段一起[Takio，K.，布卢门塔尔，D. K.，Edelman，A. M.，沃尔什，K.一、Krebs，E. G.，& Titani，K.（1985）Biochemistry 24，6028]，本工作完成了该蛋白的603个残基的序列。本文分析的氨基末端片段对应于据报道具有高度不对称形状和未知功能的结构域。二级结构计算未能提供α-螺旋或β-结构的任何证据，但聚脯氨酸II样螺旋结构是可能的。序列分析表明存在大约等量的两种亚型，其不同之处在于单个氨基酸置换。在本序列分析中遇到了意想不到的困难，由于酸不稳定的Asp-Pro键的存在和5个可分离的变体的封闭的21个残基的氨基末端肽，在Asn-Gly键的重排所产生的。
The amino acid sequence of the amino-terminal, 235-residue segment of rabbit skeletal muscle myosin light chain kinase has been determined. Together with the carboxyl-terminal segment previously described [Takio, K., Blumenthal, D. K., Edelman, A. M., Walsh, K. A., Krebs, E. G., & Titani, K. (1985) Biochemistry 24, 6028], the present work completes the 603-residue sequence of this protein. The amino-terminal segment that has been analyzed herein corresponds to a domain reported to be of highly asymmetrical shape and as yet unknown function. Secondary structure calculations failed to provide any evidence of alpha-helix or beta-structures, but polyproline II like helical structure is possible. Sequence analysis indicates the presence of approximately equal quantities of two isoforms differing in a single amino acid replacement. Unexpected difficulties were encountered in the present sequence analysis due to the presence of acid-labile Asp-Pro bonds and to five separable variants of a blocked 21-residue amino-terminal peptide, arising from rearrangement at an Asn-Gly bond.
DOI：
10.1073/pnas.78.2.848
发表时间：
1981-01-01
期刊：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子：
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作者：
SHOJI, S;PARMELEE, DC;TITANI, K
通讯作者：
TITANI, K