| http://purl.uniprot.org/citations/19008222 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19008222 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19008222 | http://www.w3.org/2000/01/rdf-schema#comment | "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 exhibits a Ca2+-induced closed to open transition like that of CaM. The Ca2+-bound C-domain contains exposed hydrophobic residues (Leu132, His134, Ile141, Ile144, and Val148) that may account for selective binding to InsP3Rs. Isothermal titration calorimetry analysis reveals a Ca2+-induced binding of the CaBP1 C-domain to the N-terminal region of InsP3R (residues 1-587), whereas CaM and the CaBP1 N-domain did not show appreciable binding. CaBP1 binding to InsP3Rs requires both the suppressor and ligand-binding core domains, but has no effect on InsP3 binding to the receptor. We propose that CaBP1 may regulate Ca2+-dependent activity of InsP3Rs by promoting structural contacts between the suppressor and core domains."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m806513200"xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m806513200"xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Li C."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Li C."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Ikura M."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Ikura M."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Palczewski K."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Palczewski K."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Chan J."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Chan J."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Mikoshiba K."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Mikoshiba K."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Haeseleer F."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Haeseleer F."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Ames J.B."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/author | "Ames J.B."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/pages | "2472-2481"xsd:string |
| http://purl.uniprot.org/citations/19008222 | http://purl.uniprot.org/core/pages | "2472-2481"xsd:string |