Calmodulin-peptide interactions: apocalmodulin binding to the myosin light chain kinase target-site.
Biochemistry
; 39(24): 7284-90, 2000 Jun 20.
Article
en En
| MEDLINE
| ID: mdl-10852728
ABSTRACT
Noncovalent binding of the synthetic peptide RS20 to calmodulin in the presence of calcium was confirmed by electrospray ionization coupled with Fourier transform ion cyclotron resonance mass spectrometry to form a complex with a 114 calmodulin/RS20/calcium stoichiometry. There was no evidence for formation of a calmodulin-RS20-Ca(2) species. The absence of calmodulin-RS20-Ca(2) would be consistent with models in which the two globular domains are coupled functionally. There was evidence that calmodulin, RS20-calmodulin without associated calcium, and calmodulin-RS20-Ca(4) existed together in solution, whereas calmodulin-calcium complexes were absent. It is proposed that calcium binding to form the calmodulin-RS20-Ca(4) complex occurs after an initial RS20-calmodulin binding event, and serves to secure the target within the calmodulin structure. The binding of more than one RS20 molecule to calmodulin was observed to induce unfolding of calmodulin.
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Base de datos:
MEDLINE
Asunto principal:
Quinasa de Cadena Ligera de Miosina
/
Proteínas de Unión a Calmodulina
/
Calmodulina
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Biochemistry
Año:
2000
Tipo del documento:
Article
País de afiliación:
Reino Unido