2hqw
From Proteopedia
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- | [[Image:2hqw.jpg|left|200px]] | + | [[Image:2hqw.jpg|left|200px]] |
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- | '''Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide''' | + | {{Structure |
+ | |PDB= 2hqw |SIZE=350|CAPTION= <scene name='initialview01'>2hqw</scene>, resolution 1.90Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2HQW is a [ | + | 2HQW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HQW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18073110 18073110] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: nr1]] | [[Category: nr1]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:20:27 2008'' |
Revision as of 15:20, 20 March 2008
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, resolution 1.90Å | |||||||
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Ligands: | |||||||
Gene: | Calm1, Calm, Cam, Cam1 (Rattus norvegicus) | ||||||
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 Thu Mar 20 17:20:27 2008
Categories: Protein complex | Rattus norvegicus | Akyol, Z. | Gakhar, L. | Hell, J H. | Shea, M A. | Sorensen, B R. | CA | 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