Non-canonical H-bonds in β-lactamases: importance of C–H···π interactions

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• 作者：P. Lavanya (1)
  Sudha Ramaiah (1)
  Anand Anbarasu (1)
  
• 关键词：C–H···π interactions ; β ; Lactamases ; Stabilization centres ; Conservation ; Solvent accessibility
• 刊名：Journal of Biological Inorganic Chemistry
• 出版年：2013
• 出版时间：June 2013
• 年：2013
• 卷：18
• 期：5
• 页码：539-545
• 全文大小：556KB
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• 作者单位：P. Lavanya (1)
  Sudha Ramaiah (1)
  Anand Anbarasu (1)
  
  1. Medical and Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore, 632014, Tamil Nadu, India
  
• ISSN：1432-1327

文摘

β-Lactamase production is the common mechanism of resistance of β-lactam antibiotics. Knowledge of inter-residue interactions in protein structures increases our understanding of protein structure and stability. We have systematically analysed the contribution of C–H···π interactions to the stability of β-lactamases. Most of the interactions are long range and most of the interacting residues are evolutionarily conserved. The occurrence of C–H···π interactions in active sites and metal binding sites is very low in β-lactamases. Hence, C–H···π interactions are important determinants of stability in β-lactamases and they may not play a significant role in specificity. The results from this study provide valuable insights for understanding the stability patterns of β-lactamases and their relation to various other environmental preferences.