Structure of a trapped intermediate of calmodulin: calcium regulation of EF-hand proteins from a new perspective.

doi:10.1016/j.jmb.2005.01.004

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Article

Structure of a trapped intermediate of calmodulin: calcium regulation of EF-hand proteins from a new perspective.

Journal of molecular biology - 11 Mar 2005

Grabarek Zenon

Abstract excerpt

Calmodulin (CaM) is a multifunctional Ca2+-binding protein that regulates the activity of many enzymes in response to changes in the intracellular Ca2+ concentration. There are two globular domains in CaM, each containing a pair of helix-loop-helix Ca2+-binding motifs called EF-hands. Ca2+-binding induces the opening of both domains thereby exposing hydrophobic pockets that provide binding sites for the target...

Topics

Binding Sites
Calcium
Calmodulin
Disulfides
Humans
Ligands
Membrane Microdomains
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Protein Binding
Protein Conformation
Troponin C

Source

Open in PubMed

Identifiers

PMID: 15713486
DOI: 10.1016/j.jmb.2005.01.004

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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