1W9E

Crystal structure of the PDZ tandem of human syntenin in complex with TNEFYF peptide

1W9E の概要

• エントリーDOI: 10.2210/pdb1w9e/pdb
• 関連するPDBエントリー: 1N99 1NTE 1OBX 1OBY 1OBZ 1R6J 1V1T 1W9O 1W9Q 1YBO
• 分子名称: SYNTENIN 1, TNEFYF PEPTIDE, BENZOIC ACID, ... (4 entities in total)
• 機能のキーワード: cell adhesion, adhesion-complex, pdz domain, scaffolding protein signaling protein
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 38619.07

構造登録者

Grembecka, J.,Cierpicki, T.,Devedjiev, Y.,Cooper, D.R.,Derewenda, U.,Derewenda, Z.S. (登録日: 2004-10-09, 公開日: 2006-03-22, 最終更新日: 2023-12-13)

主引用文献

Grembecka, J.,Cierpicki, T.,Devedjiev, Y.,Derewenda, U.,Kang, B.S.,Bushweller, J.H.,Derewenda, Z.S.
The Binding of the Pdz Tandem of Syntenin to Target Proteins.
Biochemistry, 45:3674-, 2006

PubMed Abstract: PDZ domains are among the most abundant protein modules in the known genomes. Their main function is to provide scaffolds for membrane-associated protein complexes by binding to the cytosolic, C-terminal fragments of receptors, channels, and other integral membrane proteins. Here, using both heteronuclear NMR and single crystal X-ray diffraction, we show how peptides with different sequences, including those corresponding to the C-termini of syndecan, neurexin, and ephrin B, can simultaneously bind to both PDZ domains of the scaffolding protein syntenin. The PDZ2 domain binds these peptides in the canonical fashion, and an induced fit mechanism allows for the accommodation of a range of side chains in the P(0) and P(-)(2) positions. However, binding to the PDZ1 domain requires that the target peptide assume a noncanonical conformation. These data help explain how syntenin, and perhaps other PDZ-containing proteins, may preferentially bind to dimeric and clustered targets, and provide a mechanistic explanation for the previously reported cooperative ligand binding by syntenin's two PDZ domains.

PubMed: 16533050
DOI: 10.1021/BI052225Y

実験手法

X-RAY DIFFRACTION (1.56 Å)