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

38 Citations (Scopus)

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
  • Chemistry(all)

Fingerprint

Dive into the research topics of 'Structural basis of α-fucosidase inhibition by iminocyclitols with Ki values in the micro- to picomolar range'. Together they form a unique fingerprint.

Cite this