Ontology highlight
ABSTRACT:
SUBMITTER: Laine E
PROVIDER: S-EPMC3042556 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Laine Elodie E Martínez Leandro L Blondel Arnaud A Malliavin Thérèse E TE
Biophysical journal 20101001 7
Calmodulin (CaM) is a remarkably flexible protein which can bind multiple targets in response to changes in intracellular calcium concentration. It contains four calcium-binding sites, arranged in two globular domains. The calcium affinity of CaM N-terminal domain (N-CaM) is dramatically reduced when the complex with the edema factor (EF) of Bacillus anthracis is formed. Here, an atomic explanation for this reduced affinity is proposed through molecular dynamics simulations and free energy pertu ...[more]