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Structural basis of α-fucosidase inhibition by iminocyclitols with Ki values in the micro- to picomolar range

  • Hsing Ju Wu
  • , Ching Wen Ho
  • , Tzu Ping Ko
  • , Shinde D. Popat
  • , Chun Hung Lin
  • , Andrew H.J. Wang

Research output: Contribution to journalArticlepeer-review

Abstract

"Chemical Equation Presented" Two loops were found to move inward toward the αfucosidase active site to produce a closed conformation of complexes with inhibitors with increasing Ki values from the micro- to nanomolar range. Although no further conformational changes in the two loops are observed for inhibitors with sub-nanomolar Ki values, the loops are additionally stabilized by hydrogen bonds and hydrophobic interactions.

Original languageEnglish
Pages (from-to)337-340
Number of pages4
JournalAngewandte Chemie - International Edition
Volume49
Issue number2
DOIs
Publication statusPublished - Jan 8 2010
Externally publishedYes

Keywords

  • Fucosidases
  • Iminocyclitols
  • Inhibitors
  • Slow binding

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry

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