7VEG

Understanding NH-pi interaction between Gln and Phe

7VEG の概要

• エントリーDOI: 10.2210/pdb7veg/pdb
• 分子名称: peptide, ACETYLAMINO-ACETIC ACID (2 entities in total)
• 機能のキーワード: side chain interactions, nh-pi interaction, collagen-like peptide, structural protein
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 6736.16

構造登録者

Fan, S.,Xu, F. (登録日: 2021-09-08, 公開日: 2022-10-19, 最終更新日: 2024-10-09)

主引用文献

Zhang, R.,Xu, Y.,Lan, J.,Fan, S.,Huang, J.,Xu, F.
Structural Achievability of an NH-pi Interaction between Gln and Phe in a Crystal Structure of a Collagen-like Peptide.
Biomolecules, 12:-, 2022

PubMed Abstract: NH-π interactions between polar and aromatic residues are well distributed in proteins whose stabilizing effects have been investigated in globular and fibrous proteins. In order to gain structural insights into side chain NH-π interactions, we solved a crystal structure of a collagen-like peptide containing Gln-Phe pairs. The Gln-Phe NH-π interactions were further characterized by quantum calculations, molecular simulations, and structural bioinformatics. The analyses indicated that the NH-π interactions are robust under various solvent conditions, can be distributed either on the protein surface or in its hydrophobic core and can form at a wide range of distances between residues. This study suggested that NH-π interactions can play a versatile role in protein design, including engineering hydrophobic cores, solvent accessible surfaces, and protein-protein interfaces.

PubMed: 36291642
DOI: 10.3390/biom12101433

実験手法

X-RAY DIFFRACTION (1.39 Å)