Intra- and interdomain effects due to mutation of calcium-binding sites in calmodulin.

ABSTRACT: The IQ-motif protein PEP-19, binds to the C-domain of calmodulin (CaM) with significantly different k(on) and k(off) rates in the presence and absence of Ca(2+), which could play a role in defining the levels of free CaM during Ca(2+) transients. The initial goal of the current study was to determine whether Ca(2+) binding to sites III or IV in the C-domain of CaM was responsible for affecting the kinetics of binding PEP-19. EF-hand Ca(2+)-binding sites were selectively inactivated by the common strategy of changing Asp to Ala at the X-coordination position. Although Ca(2+) binding to both sites III and IV appeared necessary for native-like interactions with PEP-19, the data also indicated that the mutations caused undesirable structural alterations as evidenced by significant changes in a

SUBMITTER: Xiong LW 

PROVIDER: S-EPMC2832960 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature