FEBS Letters 2008-06-25

Calcium-induced tripartite binding of intrinsically disordered calpastatin to its cognate enzyme, calpain.

Róbert Kiss, Zoltán Bozoky, Dénes Kovács, Gergely Róna, Péter Friedrich, Péter Dvortsák, Rüdiger Weisemann, Rudinger Weisemann, Péter Tompa, András Perczel

Index: FEBS Lett. 582(15) , 2149-54, (2008)

Full Text: HTML

Abstract

The activity of calpain is controlled by the free intracellular calcium level and by the protein's intrinsically disordered endogenous inhibitor, calpastatin, mediated by short conserved segments: subdomains A-C. The exact binding mode of calpastatin to the enzyme has until now been unclear. Our NMR data of the 141 amino acid long inhibitor, with and without calcium and calpain, have revealed structural changes and a tripartite binding mode, in which the disordered inhibitor wraps around, and contacts, the enzyme at three points, facilitated by flexible linkers. This unprecedented binding mode permits a unique combination of specificity, speed and binding strength in regulation.

Related Compounds

  • Yeast extract

Related Articles:

The mitosis-to-interphase transition is coordinated by cross talk between the SIN and MOR pathways in Schizosaccharomyces pombe.

2010-09-06

[J. Cell Biol. 190(5) , 793-805, (2010)]

LsrR quorum sensing "switch" is revealed by a bottom-up approach.

2011-09-01

[PLoS Comput. Biol. 7(9) , e1002172, (2011)]

Hypoxia modifies the feeding preferences of Drosophila. Consequences for diet dependent hypoxic survival.

2010-01-01

[BMC Physiol. 10 , 8, (2010)]

How to assess and study cell death in Dictyostelium discoideum.

2006-01-01

[Methods Mol. Biol. 346 , 535, (2006)]

Preparation, application and testing of permanent antibacterial and antiviral coatings.

2007-01-01

[Nat. Protoc. 2 , 2412, (2007)]

More Articles...