2hqw
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2hqw |SIZE=350|CAPTION= <scene name='initialview01'>2hqw</scene>, resolution 1.90Å | |PDB= 2hqw |SIZE=350|CAPTION= <scene name='initialview01'>2hqw</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hqw OCA], [http://www.ebi.ac.uk/pdbsum/2hqw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hqw RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Shea, M A.]] | [[Category: Shea, M A.]] | ||
[[Category: Sorensen, B R.]] | [[Category: Sorensen, B R.]] | ||
| - | [[Category: CA]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
[[Category: c1 casette]] | [[Category: c1 casette]] | ||
| Line 43: | Line 45: | ||
[[Category: nr1]] | [[Category: nr1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:34:08 2008'' |
Revision as of 00:34, 31 March 2008
| |||||||
| , 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
Page seeded by OCA on Mon Mar 31 03:34:08 2008
Categories: Protein complex | Rattus norvegicus | Akyol, Z. | Gakhar, L. | Hell, J H. | Shea, M A. | Sorensen, B R. | Alternative splicing | C1 casette | Calcium channel | Calmodulin | Central nervous system | Ef hand motif | Er retention signal | Globular complex | Glutamate | Ion channel | Metal binding protein | N-methyl-d-aspartate receptor | Neuronal channel | Nr1
