Preference of calcium-dependent interactions between calmodulin-like domains of calpain and calpastatin subdomains.
FEBS Lett
; 362(1): 93-7, 1995 Mar 27.
Article
em En
| MEDLINE
| ID: mdl-7698360
ABSTRACT
Calpastatin molecule contains four repeated inhibition domains, each having highly conserved internal regions A, B and C. The synthetic oligopeptides of regions A and C had no calpain inhibition activity while region B oligopeptide showed weak inhibition activity. Real-time biomolecular interaction analysis using a BIAcore instrument revealed that the bacterially expressed calmodulin-like domain of the calpain large subunit (L-CaMLD) and that of the small subunit (S-CaMLD) interacted, in a Ca(2+)-dependent fashion, preferentially with the immobilized synthetic oligopeptide of region A and that of region C, respectively. Calmodulin showed no specific binding to these oligopeptides. The tripartite structure of the calpastatin functional domain may confer the specific interactions with the protease domain and the two CaMLDs of calpain.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Ligação ao Cálcio
/
Calpaína
/
Cálcio
Limite:
Humans
Idioma:
En
Ano de publicação:
1995
Tipo de documento:
Article