2HQW: Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR NR1C1 Peptide

Citation:
Abstract
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 pocket. This 1-7 pattern was most similar to that in the CaM-MARCKS complex. Comparison of CaM-ligand wrap-around conformations identified a core tetrad of CaM C-domain residues (FLMM(C)) that contacted all ligands consistently. An identical tetrad of N-domain residues (FLMM(N)) made variable sets of contacts with ligands. This CaM-NR1C1 structure provides a foundation for designing mutants to test the role of CaM in NR1 trafficking as well as insights into how the homologous CaM domains have different roles in molecular recognition.
PDB ID: 2HQWDownload
MMDB ID: 60462
PDB Deposition Date: 2006/7/19
Updated in MMDB: 2007/12
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 2HQW: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 2HQW
Label Count Molecule
Proteins (2 molecules)
1
Calmodulin
Molecule annotation
1
Glutamate Nmda Receptor Subunit Zeta 1(Gene symbol: GRIN1)
Molecule annotation
Chemicals (4 molecules)
1
4
* Click molecule labels to explore molecular sequence information.

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