2hqw
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2hqw.jpg|left|200px]] | [[Image:2hqw.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2hqw", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2hqw| PDB=2hqw | SCENE= }} | |
| - | | | + | |
| - | | | + | |
| - | }} | + | |
'''Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide''' | '''Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide''' | ||
| Line 30: | Line 27: | ||
[[Category: Shea, M A.]] | [[Category: Shea, M A.]] | ||
[[Category: Sorensen, B R.]] | [[Category: Sorensen, B R.]] | ||
| - | [[Category: | + | [[Category: Alternative splicing]] |
| - | [[Category: | + | [[Category: C1 casette]] |
| - | [[Category: | + | [[Category: Calcium channel]] |
| - | [[Category: | + | [[Category: Calmodulin]] |
| - | [[Category: | + | [[Category: Central nervous system]] |
| - | [[Category: | + | [[Category: Ef hand motif]] |
| - | [[Category: | + | [[Category: Er retention signal]] |
| - | [[Category: | + | [[Category: Globular complex]] |
| - | [[Category: | + | [[Category: Glutamate]] |
| - | [[Category: | + | [[Category: Ion channel]] |
| - | [[Category: | + | [[Category: Metal binding protein]] |
| - | [[Category: | + | [[Category: N-methyl-d-aspartate receptor]] |
| - | [[Category: | + | [[Category: Neuronal channel]] |
| - | [[Category: | + | [[Category: Nr1]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:36:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:36, 4 May 2008
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 Sun May 4 06:36:08 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
