2APH

Crystal structure of human PGRP-IalphaC in complex with muramyl pentapeptide

2APH の概要

• エントリーDOI: 10.2210/pdb2aph/pdb
• 関連するPDBエントリー: 1SK3 1SK4 1TWQ
• 分子名称: Peptidoglycan recognition protein I-alpha, muramyl pentapeptide, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: pgrps, lys-type, peptidoglycan, complex, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 38295.39

構造登録者

Guan, R.,Roychowdjury, A.,Boons, G.,Mariuzza, R.A. (登録日: 2005-08-16, 公開日: 2006-06-27, 最終更新日: 2024-02-28)

主引用文献

Guan, R.,Brown, P.H.,Swaminathan, C.P.,Roychowdhury, A.,Boons, G.J.,Mariuzza, R.A.
Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria.
Protein Sci., 15:1199-1206, 2006

PubMed Abstract: Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors of the innate immune system that bind bacterial peptidoglycans (PGNs). We determined the crystal structure, to 2.1 A resolution, of the C-terminal PGN-binding domain of human PGRP-I alpha in complex with a muramyl pentapeptide (MPP) from Gram-positive bacteria containing a complete peptide stem (L-Ala-D-isoGln-L-Lys-D-Ala-D-Ala). The structure reveals important features not observed previously in the complex between PGRP-I alpha and a muramyl tripeptide lacking D-Ala at stem positions 4 and 5. Most notable are ligand-induced structural rearrangements in the PGN-binding site that are essential for entry of the C-terminal portion of the peptide stem and for locking MPP in the binding groove. We propose that similar structural rearrangements to accommodate the PGN stem likely characterize many PGRPs, both mammalian and insect.

PubMed: 16641493
DOI: 10.1110/ps.062077606

実験手法

X-RAY DIFFRACTION (2.1 Å)