Ontology highlight
ABSTRACT:
SUBMITTER: Li C
PROVIDER: S-EPMC2629100 | biostudies-literature | 2009 Jan
REPOSITORIES: biostudies-literature
Li Congmin C Chan Jenny J Haeseleer Franciose F Mikoshiba Katsuhiko K Palczewski Krzysztof K Ikura Mitsuhiko M Ames James B JB
The Journal of biological chemistry 20081113 4
Calcium-binding protein 1 (CaBP1), a neuron-specific member of the calmodulin (CaM) superfamily, modulates Ca2+-dependent activity of inositol 1,4,5-trisphosphate receptors (InsP3Rs). Here we present NMR structures of CaBP1 in both Mg2+-bound and Ca2+-bound states and their structural interaction with InsP3Rs. CaBP1 contains four EF-hands in two separate domains. The N-domain consists of EF1 and EF2 in a closed conformation with Mg2+ bound at EF1. The C-domain binds Ca2+ at EF3 and EF4, and exhi ...[more]