Ontology highlight
ABSTRACT:
SUBMITTER: Kumar V
PROVIDER: S-EPMC3558517 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Kumar Veerendra V Chichili Vishnu Priyanka Reddy VP Tang Xuhua X Sivaraman J J
PloS one 20130129 1
Calmodulin (CaM) is a highly conserved eukaryotic protein that binds specifically to more than 100 target proteins in response to calcium (Ca(2+)) signal. CaM adopts a considerable degree of structural plasticity to accomplish this physiological role; however, the nature and extent of this plasticity remain to be fully understood. Here, we report the crystal structure of a novel trans conformation of ligand-free CaM where the relative disposition of two lobes of CaM is different, a conformation ...[more]