7VEG

Understanding NH-pi interaction between Gln and Phe

Summary for 7VEG

• Entry DOI: 10.2210/pdb7veg/pdb
• Descriptor: peptide, ACETYLAMINO-ACETIC ACID (2 entities in total)
• Functional Keywords: side chain interactions, nh-pi interaction, collagen-like peptide, structural protein
• Biological source: Homo sapiens
• Total number of polymer chains: 3
• Total formula weight: 6736.16

Authors

Fan, S.,Xu, F. (deposition date: 2021-09-08, release date: 2022-10-19, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.39 Å)