1QAU

UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX

1QAU の概要

• エントリーDOI: 10.2210/pdb1qau/pdb
• 分子名称: NEURONAL NITRIC OXIDE SYNTHASE (RESIDUES 1-130) (2 entities in total)
• 機能のキーワード: beta-finger, oxidoreductase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cell membrane, sarcolemma; Peripheral membrane protein (By similarity): P29476
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12032.88

構造登録者

Hillier, B.J.,Christopherson, K.S.,Prehoda, K.E.,Bredt, D.S.,Lim, W.A. (登録日: 1999-03-29, 公開日: 1999-05-04, 最終更新日: 2024-02-14)

主引用文献

Hillier, B.J.,Christopherson, K.S.,Prehoda, K.E.,Bredt, D.S.,Lim, W.A.
Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex.
Science, 284:812-815, 1999

PubMed Abstract: The PDZ protein interaction domain of neuronal nitric oxide synthase (nNOS) can heterodimerize with the PDZ domains of postsynaptic density protein 95 and syntrophin through interactions that are not mediated by recognition of a typical carboxyl-terminal motif. The nNOS-syntrophin PDZ complex structure revealed that the domains interact in an unusual linear head-to-tail arrangement. The nNOS PDZ domain has two opposite interaction surfaces-one face has the canonical peptide binding groove, whereas the other has a beta-hairpin "finger." This nNOS beta finger docks in the syntrophin peptide binding groove, mimicking a peptide ligand, except that a sharp beta turn replaces the normally required carboxyl terminus. This structure explains how PDZ domains can participate in diverse interaction modes to assemble protein networks.

PubMed: 10221915
DOI: 10.1126/science.284.5415.812

実験手法

X-RAY DIFFRACTION (1.25 Å)