FEBS Letters | |
Skeletal muscle myosin light chain kinase | |
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
【 预 览 】
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RO201912020284427ZK.pdf | 739KB | download |