3WN8

Crystal Structure of Collagen-Model Peptide, (POG)3-PRG-(POG)4

3WN8 の概要

• エントリーDOI: 10.2210/pdb3wn8/pdb
• 関連するPDBエントリー: 3B0S
• 分子名称: collagen-like peptide (2 entities in total)
• 機能のキーワード: collagen-helix, hsp47 binding, structural protein
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 6601.03

構造登録者

Okuyama, K.,Haga, M.,Noguchi, K.,Tanaka, T. (登録日: 2013-12-06, 公開日: 2014-08-13, 最終更新日: 2023-11-08)

主引用文献

Okuyama, K.,Haga, M.,Noguchi, K.,Tanaka, T.
Preferred side-chain conformation of arginine residues in a triple-helical structure.
Biopolymers, 101:1000-1009, 2014

PubMed Abstract: The crystal structure of the triple-helical peptide (Pro-Hyp-Gly)3 -Pro-Arg-Gly-(Pro-Hyp-Gly)4 (POG3-PRG-POG4) was determined at 1.45 Å resolution. POG3-PRG-POG4 was designed to permit investigation of the side-chain conformation of the Arg residues in a triple-helical structure. Because of the alternative structure of one of three Arg residues, four side-chain conformations were observed in an asymmetric unit. Among them, three adopt a ttg(-) t conformation and the other adopts a tg(-) g(-) t conformation. A statistical analysis of 80 Arg residues in various triple-helical peptides showed that, unlike those in globular proteins, they preferentially adopt a tt conformation for χ1 and χ2 , as observed in POG3-PRG-POG4. This conformation permits van der Waals contacts between the side-chain atoms of Arg and the main-chain atoms of the adjacent strand in the same molecule. Unlike many other host-guest peptides, in which there is a significant difference between the helical twists in the guest and the host peptides, POG3-PRG-POG4 shows a marked difference between the helical twists in the N-terminal peptide and those in the C-terminal peptide, separated near the Arg residue. This suggested that the unique side-chain conformation of the Arg residue affects not only the conformation of the guest peptide, but also the conformation of the peptide away from the Arg residue.

PubMed: 24615532
DOI: 10.1002/bip.22478

実験手法

X-RAY DIFFRACTION (1.45 Å)