Ontology highlight
ABSTRACT:
SUBMITTER: Ataman ZA
PROVIDER: S-EPMC2246159 | biostudies-literature | 2007 Dec
REPOSITORIES: biostudies-literature
Ataman Zeynep Akyol ZA Gakhar Lokesh L Sorensen Brenda R BR Hell Johannes W JW Shea Madeline A MA
Structure (London, England : 1993) 20071201 12
Calmodulin (CaM) regulates tetrameric N-methyl-D-aspartate receptors (NMDARs) by binding tightly to the C0 and C1 regions of its NR1 subunit. A crystal structure (2HQW; 1.96 A) of calcium-saturated CaM bound to NR1C1 (peptide spanning 875-898) showed that NR1 S890, whose phosphorylation regulates membrane localization, was solvent protected, whereas the endoplasmic reticulum retention motif was solvent exposed. NR1 F880 filled the CaM C-domain pocket, whereas T886 was closest to the N-domain poc ...[more]