High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: mimicry of carbohydrate substrate.

@article{Houston2002HighresolutionSO,
  title={High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: mimicry of carbohydrate substrate.},
  author={Douglas R. Houston and Kazuro Shiomi and Noriko Arai and Satoshi Ōmura and Martin G. Peter and Andreas Turberg and Bj\ornar Synstad and Vincent G H Eijsink and Daan M F van Aalten},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2002},
  volume={99 14},
  pages={9127-32}
}
Over the past years, family 18 chitinases have been validated as potential targets for the design of drugs against human pathogens that contain or interact with chitin during their normal life cycles. Thus far, only one potent chitinase inhibitor has been described in detail, the pseudotrisaccharide allosamidin. Recently, however, two potent natural-product cyclopentapeptide chitinase inhibitors, argifin and argadin, were reported. Here, we describe high-resolution crystal structures that… CONTINUE READING

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Enzymology. Lineweaver–Burk plots illustrating inhibition of wildtype (WT) ChiB and the W220A mutant. Km ChiB 33 M, kcat ChiB 15 s 1, Km W220A 97 M, and kcat W220A 1.0 s 1

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