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From the same journal

Three dimensional structure of a bacterial α-l-fucosidase with a 5-membered iminocyclitol inhibitor

Research output: Contribution to journalArticle

Published copy (DOI)

Author(s)

  • D.W. Wright
  • A.J. Moreno-Vargas
  • A.T. Carmona
  • I. Robina
  • G.J. Davies

Department/unit(s)

Publication details

JournalBioorganic & Medicinal Chemistry
DatePublished - 15 Aug 2013
Issue number16
Volume21
Pages (from-to)4751-4754
Original languageEnglish

Abstract

Fucosidases, enzymes that cleave fucose from the non-reducing end of a glycan, represent promising medicinal targets reflecting their roles in cancer metastasis, inflammation, host-parasite interactions and the lysosomal storage disorder fucosidosis. The X-ray crystal structures of Bacteroides thetaiotaomicron GH29 α-l-fucosidase (BtFuc2970) in a new crystal form (at a resolution of 1.59 Å) and liganded with a 5-membered iminocyclitol inhibitor (1.73 Å) are reported herein. The 5-membered iminocyclitol binds in a E conformation, mimicking the proposed H half chair transition-state of the enzyme catalysed reaction, and its K for BtFuc2970 was determined as 2 μM. Structural analysis of fucosidase inhibition through 5-membered iminocyclitols will aid in the rational design of more potent fucosidase inhibitors for treatment of a range of medical conditions.

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