2HQW
Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide
Summary for 2HQW
| Entry DOI | 10.2210/pdb2hqw/pdb |
| Descriptor | Calmodulin, Glutamate NMDA receptor subunit zeta 1, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | calmodulin, ef hand motif, globular complex, ion channel, nr1, c1 casette, n-methyl-d-aspartate receptor, glutamate, central nervous system, neuronal channel, calcium channel, er retention signal, metal binding protein |
| Biological source | Rattus norvegicus (Norway rat) More |
| Cellular location | Cytoplasm, cytoskeleton, spindle: P62161 Cell membrane; Multi-pass membrane protein (By similarity): Q05586 |
| Total number of polymer chains | 2 |
| Total formula weight | 19646.95 |
| Authors | Akyol, Z.,Gakhar, L.,Sorensen, B.R.,Hell, J.H.,Shea, M.A. (deposition date: 2006-07-19, release date: 2007-11-13, Last modification date: 2024-02-14) |
| Primary citation | Ataman, Z.A.,Gakhar, L.,Sorensen, B.R.,Hell, J.W.,Shea, M.A. The NMDA Receptor NR1 C1 Region Bound to Calmodulin: Structural Insights into Functional Differences between Homologous Domains. Structure, 15:1603-1617, 2007 Cited by PubMed 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. PubMed: 18073110DOI: 10.1016/j.str.2007.10.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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