Domain swapping and different oligomeric States for the complex between calmodulin and the calmodulin-binding domain of calcineurin a.

ABSTRACT:

Background

Calmodulin (CaM) is a ubiquitously expressed calcium sensor that engages in regulatory interactions with a large number of cellular proteins. Previously, a unique mode of CaM target recognition has been observed in the crystal structure of a complex between CaM and the CaM-binding domain of calcineurin A.

Methodology/principal findings

We have solved a high-resolution crystal structure of a complex between CaM and the CaM-binding domain of calcineurin A in a novel crystal form, which shows a dimeric assembly of calmodulin, as observed before in the crystal state. We note that the conformation of CaM in this complex is very similar to that of unliganded CaM, and a detailed analysis revels that the CaM-binding motif in calcineurin A is of a novel '1-11' type. Howeve

SUBMITTER: Majava V 

PROVIDER: S-EPMC2671406 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature