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Crystal Structures of Trypanosoma brucei Oligopeptidase B Broaden the Paradigm of Catalytic Regulation in Prolyl Oligopeptidase Family Enzymes

DOI: 10.1371/journal.pone.0079349 DOI Help
PMID: 24265767 PMID Help

Authors: Peter Canning (University of Oxford) , Dean Rea (University of Warwick) , Rory E. Morty (Max Planck Institute for Heart and Lung Research) , Vilmos Fulop (Department of Biological Sciences, University of Warwick) , Alexander Wlodawer
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Plos One , VOL 8 (11)

State: Published (Approved)
Published: November 2013
Diamond Proposal Number(s): 310

Open Access Open Access

Abstract: Oligopeptidase B cleaves after basic amino acids in peptides up to 30 residues. As a virulence factor in bacteria and trypanosomatid pathogens that is absent in higher eukaryotes, this is a promising drug target. Here we present ligand-free open state and inhibitor-bound closed state crystal structures of oligopeptidase B from Trypanosoma brucei, the causative agent of African sleeping sickness

Journal Keywords: Catalytic; Crystallography; X-Ray; Models; Molecular; Protein; Quaternary; Serine; Trypanosoma brucei brucei

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

Other Facilities: Yes ID29, ESRF, France