Preference of calcium-dependent interactions between calmodulin-like domains of calpain and calpastatin subdomains.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Takano E,Ma H,Yang HQ,Maki M,Hatanaka M

doi

10.1016/0014-5793(95)00219-y

subject

Has Abstract

pub_date

1995-03-27 00:00:00

pages

93-7

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)00219-Y

journal_volume

362

pub_type

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