title: Cation-π interactions in β-lactamases: the role in structural stability.
abstract: β-lactam group of antibiotics is the most widely used therapeutic molecules for treating bacterial infections. The main mode of bacterial resistance to β-lactams is by β-lactamases. In the present study, we report our results on the role of cation-π interactions in β-lactamases and their environmental preferences. The number of interactions formed by arginine is higher than lysine in the cationic group, while tyrosine is comparatively higher than phenylalanine and tryptophan in the π group. Our results indicate that cation-π interactions might play an important role in the global conformational stability of β-lactamases.
authors.affiliation: Medical and Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore, 632014, Tamil Nadu, India.
authors.forename: P
authors.initials: P
authors.lastname: Lavanya
authors.forename: Sudha
authors.initials: S
authors.lastname: Ramaiah
authors.forename: Anand
authors.initials: A
authors.lastname: Anbarasu
mesh_terms: D001120:Arginine / Q000737:chemistry; D001419:Bacteria / Q000201:enzymology; D020134:Catalytic Domain; D002412:Cations / Q000737:chemistry*; D004795:Enzyme Stability; D008239:Lysine / Q000737:chemistry; D010649:Phenylalanine / Q000737:chemistry; D011485:Protein Binding; D025941:Protein Interaction Mapping; D017433:Protein Structure, Secondary; D012997:Solvents / Q000737:chemistry; D014364:Tryptophan / Q000737:chemistry; D001618:beta-Lactamases / Q000737:chemistry*
chemical_list: D002412:Cations; D012997:Solvents; D010649:Phenylalanine; D014364:Tryptophan; D001120:Arginine; D001618:beta-Lactamases; D008239:Lysine