Rational and computational design of stabilized variants of cyanovirin-N that retain affinity and specificity for glycan ligands.

@article{Patsalo2011RationalAC,
  title={Rational and computational design of stabilized variants of cyanovirin-N that retain affinity and specificity for glycan ligands.},
  author={Vadim Patsalo and Daniel P Raleigh and David F. Green},
  journal={Biochemistry},
  year={2011},
  volume={50 49},
  pages={10698-712}
}
Cyanovirin-N (CVN) is an 11 kDa pseudosymmetric cyanobacterial lectin that has been shown to inhibit infection by the human immunodeficiency virus by binding to high-mannose oligosaccharides on the surface of the viral envelope glycoprotein gp120. In this work, we describe rationally designed CVN variants that stabilize the protein fold while maintaining high affinity and selectivity for their glycan targets. Poisson-Boltzmann calculations and protein repacking algorithms were used to select… CONTINUE READING
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