Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases

@inproceedings{Adamski2017SystematicSA,
  title={Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases},
  author={Carolyn J. Adamski and Timothy G. Palzkill},
  booktitle={BMC Biochemistry},
  year={2017}
}
The production of β-lactamases by bacteria is the most common mechanism of resistance to the widely prescribed β-lactam antibiotics. β-lactamase inhibitory protein (BLIP) competitively inhibits class A β-lactamases via two binding loops that occlude the active site. It has been shown that BLIP Tyr50 is a specificity determinant in that substitutions at this position result in large differential changes in the relative affinity of BLIP for class A β-lactamases. In this study, the effect of… CONTINUE READING
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