Skeletal muscle myosin light chain kinase

FEBS Letters

Heilmeyer, Ludwig M.G.¹  Mayr, Georg W.¹ 

[1] Institut für Physiologische Chemie, Lehrstuhl I, Ruhr-Universität, Universitätsstraße 150, 4630 Bochum 1, FRG

关键词: Myosin light chain kinase;    Calmodulin;    Proteolytic fragment;    Structural model;   

DOI  :  10.1016/0014-5793(83)80552-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A hydrodynamic, enzymatic and CD spectroscopic study of skeletal muscle myosin light chain kinase, three proteolytic fragments and corresponding complexes with calmodulin was performed. A refined shape model was built for the enzyme. It was shown that a head-and-tail structure is formed from two major fragments which are aligned end-to-end. The one fragment (M _r 36 000) is compact, of high α-helix content and contains the catalytic center with the light chain and the calmodulin binding domains. The other fragment (M _r 33 000) with unknown function is asymmetric (a/b ⪢ 10), of low α-helix and of unusually high proline content.

【 授权许可】

Unknown