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Skeletal muscle myosin light chain kinase
Author(s) -
Mayr Georg W.,
Heilmeyer Ludwig M.G.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80552-3
Subject(s) - myosin light chain kinase , calmodulin , myosin , immunoglobulin light chain , skeletal muscle , chemistry , biophysics , enzyme , helix (gastropod) , biochemistry , alpha helix , stereochemistry , protein structure , biology , anatomy , antibody , immunology , ecology , snail
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.