2EJY

Solution structure of the p55 PDZ T85C domain complexed with the glycophorin C F127C peptide

2EJY の概要

• エントリーDOI: 10.2210/pdb2ejy/pdb
• 関連するPDBエントリー: 2EV8
• 分子名称: 55 kDa erythrocyte membrane protein, Glycophorin C (2 entities in total)
• 機能のキーワード: gpc, maguk, p55, pdz, membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Peripheral membrane protein: Q00013; Cell membrane; Single-pass type III membrane protein: P04921
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12296.13

構造登録者

Kusunoki, H.,Kohno, T. (登録日: 2007-03-22, 公開日: 2008-02-12, 最終更新日: 2024-11-20)

主引用文献

Kusunoki, H.,Kohno, T.
Structural insight into the interaction between the p55 PDZ domain and glycophorin C
Biochem.Biophys.Res.Commun., 359:972-978, 2007

PubMed Abstract: p55, a member of the membrane-associated guanylate kinase family, includes a PDZ domain that specifically interacts with the C-terminal region of glycophorin C in the ternary complex of p55, protein 4.1 and glycophorin C. Here we present the first NMR-derived complex structure of the p55 PDZ domain and the C-terminal peptide of glycophorin C, obtained by using a threonine to cysteine (T85C) mutant of the p55 PDZ domain and a phenylalanine to cysteine (F127C) mutant of the glycophorin C peptide. Our NMR results revealed that the two designed mutant molecules retain the specific interaction manner that exists between the wild type molecules and can facilitate the structure determination by NMR, due to the stable complex formation via an intermolecular disulfide bond. The complex structure provides insight into the specific interaction of the p55 PDZ domain with the two key residues, Ile128 and Tyr126, of glycophorin C.

PubMed: 17572384
DOI: 10.1016/j.bbrc.2007.05.215

実験手法

SOLUTION NMR