1M5Z

The PDZ7 of Glutamate Receptor Interacting Protein Binds to its Target via a Novel Hydrophobic Surface Area

1M5Z の概要

• エントリーDOI: 10.2210/pdb1m5z/pdb
• NMR情報: BMRB: 5499
• 分子名称: AMPA receptor interacting protein (1 entity in total)
• 機能のキーワード: six beta-strands and two alpha-helices, protein binding
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm: P97879
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9979.45

構造登録者

Feng, W.,Fan, J.,Jiang, M.,Shi, Y.,Zhang, M. (登録日: 2002-07-11, 公開日: 2002-11-06, 最終更新日: 2024-05-29)

主引用文献

Feng, W.,Fan, J.-S.,Jiang, M.,Shi, Y.-W.,Zhang, M.
The PDZ7 of Glutamate Receptor Interacting Protein Binds to its Target via a Novel Hydrophobic Surface Area
J.Biol.Chem., 277:41140-41146, 2002

PubMed Abstract: Glutamate receptor interacting protein 1 (GRIP1) is a scaffold protein composed of seven PDZ (Postsynaptic synaptic density-95/Discs large/Zona occludens-1) domains. The protein plays important roles in the synaptic targeting of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors. The interaction between GRIP1 PDZ7 and a Ras guanine nucleotide exchange factor, GRASP-1, regulates synaptic distribution of AMPA receptors. Here, we describe the three-dimensional structure of GRIP1 PDZ7 determined by NMR spectroscopy. GRIP1 PDZ7 contains a closed carboxyl group-binding pocket and a narrow alphaB/betaB-groove that is not likely to bind to classical PDZ ligands. Unexpectedly, GRIP1 PDZ7 contains a large solvent-exposed hydrophobic surface at a site distinct from the conventional ligand-binding alphaB/betaB-groove. NMR titration experiments show that GRIP1 PDZ7 binds to GRASP-1 via this hydrophobic surface. Our data uncover a novel PDZ domain-mediated protein interaction mode that may be responsible for multimerization of other PDZ domain-containing scaffold proteins.

PubMed: 12196542
DOI: 10.1074/jbc.M207206200

実験手法

SOLUTION NMR