Skeletal muscle myosin light chain kinase. A refined structural model.
FEBS Lett
; 157(2): 225-31, 1983 Jul 04.
Article
em En
| MEDLINE
| ID: mdl-6688051
ABSTRACT
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 (Mr 36000) is compact, of high alpha-helix content and contains the catalytic center with the light chain and the calmodulin binding domains. The other fragment (Mr 33000) with unknown function is asymmetric (a/b greater than 10), of low alpha-helix and of unusually high proline content.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Quinases
/
Modelos Químicos
/
Músculos
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Ano de publicação:
1983
Tipo de documento:
Article