Specificity and cooperativity at β-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions.

@article{Hanes2011SpecificityAC,
  title={Specificity and cooperativity at β-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions.},
  author={Melinda S. Hanes and Kimberly A. Reynolds and Case McNamara and Partho Ghosh and Robert A. Bonomo and Jack F. Kirsch and Tracy M. Handel},
  journal={Proteins},
  year={2011},
  volume={79 4},
  pages={
          1267-76
        }
}
Establishing a quantitative understanding of the determinants of affinity in protein-protein interactions remains challenging. For example, TEM-1/β-lactamase inhibitor protein (BLIP) and SHV-1/BLIP are homologous β-lactamase/β-lactamase inhibitor protein complexes with disparate K(d) values (3 nM and 2 μM, respectively), and a single substitution, D104E in SHV-1, results in a 1000-fold enhancement in binding affinity. In TEM-1, E104 participates in a salt bridge with BLIP K74, whereas the… CONTINUE READING

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