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2hqw

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{{STRUCTURE_2hqw| PDB=2hqw | SCENE= }}
{{STRUCTURE_2hqw| PDB=2hqw | SCENE= }}
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'''Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide'''
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===Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 18073110 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18073110}}
==About this Structure==
==About this Structure==
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[[Category: Neuronal channel]]
[[Category: Neuronal channel]]
[[Category: Nr1]]
[[Category: Nr1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:36:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:58:24 2008''

Revision as of 10:58, 27 July 2008

Image:2hqw.png

Template:STRUCTURE 2hqw

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

Template:ABSTRACT PUBMED 18073110

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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