2HQW

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

2HQW の概要

• エントリーDOI: 10.2210/pdb2hqw/pdb
• 分子名称: Calmodulin, Glutamate NMDA receptor subunit zeta 1, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, spindle: P62161; Cell membrane; Multi-pass membrane protein (By similarity): Q05586
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19646.95

構造登録者

Akyol, Z.,Gakhar, L.,Sorensen, B.R.,Hell, J.H.,Shea, M.A. (登録日: 2006-07-19, 公開日: 2007-11-13, 最終更新日: 2024-02-14)

主引用文献

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

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: 18073110
DOI: 10.1016/j.str.2007.10.012

実験手法

X-RAY DIFFRACTION (1.9 Å)