Multiple interactions of the 'transducer' govern its function in calpain activation by Ca2+

Zoltán Bozóky, Anita Alexa, Peter Tompa, P. Friedrich

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Typical calpains in mammals become activated on binding of 8-12 Ca 2+ ions per enzyme molecule, giving an example of integrated, manifold regulation by calcium. Besides two identified Ca2+ sites in catalytic domain II and several EF-hand motifs in domains IV and VI, an acidic loop in the centrally positioned domain III seems to harbour Ca2+. The mediator of distant Ca2+-induced structural transitions is an elongated structural element, the 'transducer'. By site-directed mutagenesis along the transducer, we have generated various forms of rat m-calpain in which critical intramolecular interactions, as judged from the X-ray structure, would be abolished or modified. The kinetic parameters of these mutant enzymes support a model featuring shrinkage of transducer as a contributor to structural changes involved in calpain activation.

Original languageEnglish
Pages (from-to)741-744
Number of pages4
JournalBiochemical Journal
Volume388
Issue number3
DOIs
Publication statusPublished - Jun 15 2005

Fingerprint

Calpain
Transducers
Chemical activation
EF Hand Motifs
Mutagenesis
Mammals
Enzymes
Ports and harbors
Site-Directed Mutagenesis
Kinetic parameters
Rats
Catalytic Domain
X-Rays
Ions
Calcium
X rays
Molecules

Keywords

  • Calcium
  • Calpain
  • Extended transducer
  • Intramolecular signal propagation
  • Kinetic analysis
  • Site-directed mutagenesis

ASJC Scopus subject areas

  • Biochemistry

Cite this

Multiple interactions of the 'transducer' govern its function in calpain activation by Ca2+. / Bozóky, Zoltán; Alexa, Anita; Tompa, Peter; Friedrich, P.

In: Biochemical Journal, Vol. 388, No. 3, 15.06.2005, p. 741-744.

Research output: Contribution to journalArticle

Bozóky, Zoltán ; Alexa, Anita ; Tompa, Peter ; Friedrich, P. / Multiple interactions of the 'transducer' govern its function in calpain activation by Ca2+. In: Biochemical Journal. 2005 ; Vol. 388, No. 3. pp. 741-744.
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