3W9Y

Crystal structure of the human DLG1 guanylate kinase domain

3W9Y の概要

• エントリーDOI: 10.2210/pdb3w9y/pdb
• 分子名称: Disks large homolog 1 (2 entities in total)
• 機能のキーワード: guanylate kinase, molecular scaffold, peptide binding, cell membrane, peptide binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23404.50

構造登録者

Mori, S.,Tezuka, Y.,Arakawa, A.,Handa, N.,Shirouzu, M.,Akiyama, T.,Yokoyama, S. (登録日: 2013-04-18, 公開日: 2013-06-26, 最終更新日: 2023-12-06)

主引用文献

Mori, S.,Tezuka, Y.,Arakawa, A.,Handa, N.,Shirouzu, M.,Akiyama, T.,Yokoyama, S.
Crystal structure of the guanylate kinase domain from discs large homolog 1 (DLG1/SAP97)
Biochem.Biophys.Res.Commun., 435:334-338, 2013

PubMed Abstract: Discs large homolog 1 (DLG1/SAP97) is involved in the development and regulation of neuronal and immunological synapses. DLG1 is a member of the membrane associated guanylate kinase (MAGUK) family of proteins, which function as molecular scaffolds. The C-terminal guanylate kinase (GK) domain of DLG1 binds peptides with a phosphorylated serine residue. In this study, we solved the crystal structure of the GK domain of human DLG1. The C-terminal tail of DLG1 is bound to the peptide-binding site of an adjacent symmetry-related DLG1 GK molecule. The binding direction of the C-terminal tail to the peptide-binding site is opposite to that of the phosphorylated LGN peptide in complex with the rat DLG1 GK domain. The C-terminal tail forms a 310 helix, which is also different from the conformation of the phosphorylated LGN peptide. Nevertheless, the side chain interactions of the C-terminal tail with the DLG1 GK domain are similar to those of the phosphorylated LGN peptide.

PubMed: 23624197
DOI: 10.1016/j.bbrc.2013.04.056

実験手法

X-RAY DIFFRACTION (2.2 Å)