2hqw

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spinqualitylabelsall models PDB ID 2hqw Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.90Å
Ligands:
Gene:	Calm1, Calm, Cam, Cam1 (Rattus norvegicus)
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide

Overview

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.

About this Structure

2HQW is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

The NMDA receptor NR1 C1 region bound to calmodulin: structural insights into functional differences between homologous domains., Ataman ZA, Gakhar L, Sorensen BR, Hell JW, Shea MA, Structure. 2007 Dec;15(12):1603-17. PMID:18073110

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