Conserved mode of peptidomimetic inhibition and substrate recognition of human cytomegalovirus protease

@article{Tong1998ConservedMO,
  title={Conserved mode of peptidomimetic inhibition and substrate recognition of human cytomegalovirus protease},
  author={Liang Tong and Chungeng Qian and M J Massariol and Robert D{\'e}ziel and Christiane Yoakim and Lisette Lagac{\'e}},
  journal={Nature Structural Biology},
  year={1998},
  volume={5},
  pages={819-826}
}
Human cytomegalovirus (HCMV) protease belongs to a new class of serine proteases, with a unique polypeptide backbone fold. The crystal structure of the protease in complex with a peptidomimetic inhibitor (based on the natural substrates and covering the P4 to P1' positions) has been determined at 2.7 Å resolution. The inhibitor is bound in an extended conformation, forming an anti-parallel ß-sheet with the protease. The P3 and P1 side chains are less accessible to solvent, whereas the P4 and P2… CONTINUE READING

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