1TWQ

Crystal structure of the C-terminal PGN-binding domain of human PGRP-Ialpha in complex with PGN analog muramyl tripeptide

1TWQ の概要

• エントリーDOI: 10.2210/pdb1twq/pdb
• 関連するPDBエントリー: 1SK3 1SK4
• 分子名称: peptidoglycan recognition protein-I-alpha, muramyl tripeptide, NICKEL (II) ION, ... (5 entities in total)
• 機能のキーワード: crystal structure; complex; pgrp; pgrp-ialpha; pgn analog, immune system, membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18968.17

構造登録者

Guan, R.,Roychowdury, A.,Boons, G.-A.,Mariuzza, R.A. (登録日: 2004-07-01, 公開日: 2004-12-14, 最終更新日: 2024-02-28)

主引用文献

Guan, R.,Roychowdhury, A.,Ember, B.,Kumar, S.,Boons, G.-A.,Mariuzza, R.A.
Structural basis for peptidoglycan binding by peptidoglycan recognition proteins
Proc.Natl.Acad.Sci.USA, 101:17168-17173, 2004

PubMed Abstract: Peptidoglycan (PGN) recognition proteins (PGRPs) are pattern-recognition receptors of the innate immune system that bind and, in some cases, hydrolyze bacterial PGNs. We determined the crystal structure, at 2.30-A resolution, of the C-terminal PGN-binding domain of human PGRP-Ialpha in complex with a muramyl tripeptide representing the core of lysine-type PGNs from Gram-positive bacteria. The peptide stem of the ligand is buried at the deep end of a long binding groove, with N-acetylmuramic acid situated in the middle of the groove, whose shallow end can accommodate a linked N-acetylglucosamine. Although most interactions are with the peptide, the glycan moiety also seems to be essential for specific recognition by PGRPs. Conservation of key PGN-contacting residues shows that all PGRPs employ this basic PGN-binding mode. The structure pinpoints variable residues that likely mediate discrimination between lysine- and diaminopimelic acid-type PGNs. We also propose a mechanism for PGN hydrolysis by Zn(2+)-containing PGRPs.

PubMed: 15572450
DOI: 10.1073/pnas.0407856101

実験手法

X-RAY DIFFRACTION (2.3 Å)