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Structural and functional insight into human O-GlcNAcase
Authors:
Christian
Roth
(University of York)
,
Sherry
Chan
(University of York)
,
Wendy A.
Offen
(University of York)
,
Glyn R.
Hemsworth
(University of York)
,
Lianne I.
Willems
(Simon Fraser University)
,
Dustin T.
King
(Simon Fraser University)
,
Vimal
Varghese
(Simon Fraser University)
,
Robert
Britton
(Simon Fraser University)
,
David J.
Vocadlo
(Simon Fraser University)
,
Gideon J.
Davies
(University of York)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Nature Chemical Biology
, VOL 258
State:
Published (Approved)
Published:
March 2017
Diamond Proposal Number(s):
1221
,
7864
,
9948
Abstract: O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value.
Journal Keywords: Carbohydrates; Drug discovery; Enzymes; X-ray crystallography
Diamond Keywords: Alzheimer's Disease; Enzymes
Subject Areas:
Biology and Bio-materials,
Chemistry,
Medicine
Instruments:
I02-Macromolecular Crystallography
,
I03-Macromolecular Crystallography
,
I24-Microfocus Macromolecular Crystallography
Added On:
06/04/2017 10:10
Discipline Tags:
Neurodegenerative Diseases
Non-Communicable Diseases
Health & Wellbeing
Biochemistry
Neurology
Chemistry
Structural biology
Drug Discovery
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)