Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants.

@article{Telmer2003InsightsIT,
  title={Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants.},
  author={Patrick G. Telmer and Brian H. Shilton},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 36},
  pages={34555-67}
}
The affinity of maltose-binding protein (MBP) for maltose and related carbohydrates was greatly increased by removal of groups in the interface opposite the ligand binding cleft. The wild-type protein has a KD of 1200 nM for maltose; mutation of residues Met-321 and Gln-325, both to alanine, resulted in a KD for maltose of 70 nM; deletion of 4 residues, Glu-172, Asn-173, Lys-175, and Tyr-176, which are part of a poorly ordered loop, results in a KD for maltose of 110 nM. Combining the mutations… CONTINUE READING

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