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Structural and functional insight into human O-GlcNAcase

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Structural and functional insight into human O-GlcNAcase. / Roth, Christian; Chan, Oi Yi; Offen, Wendy Anne; Hemsworth, Glyn Robert; Willems, Lianne Irene; King, Dustin T.; Varghese, Vimal; Britton, Robert; Vocadlo, David J.; Davies, Gideon John.

In: NATURE CHEMICAL BIOLOGY, Vol. 13, No. 6, 01.06.2017, p. 610-612.

Research output: Contribution to journal › Article › peer-review

Harvard

Roth, C, Chan, OY, Offen, WA, Hemsworth, GR, Willems, LI, King, DT, Varghese, V, Britton, R, Vocadlo, DJ & Davies, GJ 2017, 'Structural and functional insight into human O-GlcNAcase', NATURE CHEMICAL BIOLOGY, vol. 13, no. 6, pp. 610-612. https://doi.org/10.1038/nchembio.2358

APA

Roth, C., Chan, O. Y., Offen, W. A., Hemsworth, G. R., Willems, L. I., King, D. T., Varghese, V., Britton, R., Vocadlo, D. J., & Davies, G. J. (2017). Structural and functional insight into human O-GlcNAcase. NATURE CHEMICAL BIOLOGY, 13(6), 610-612. https://doi.org/10.1038/nchembio.2358

Vancouver

Roth C, Chan OY, Offen WA, Hemsworth GR, Willems LI, King DT et al. Structural and functional insight into human O-GlcNAcase. NATURE CHEMICAL BIOLOGY. 2017 Jun 1;13(6):610-612. https://doi.org/10.1038/nchembio.2358

Author

Roth, Christian ; Chan, Oi Yi ; Offen, Wendy Anne ; Hemsworth, Glyn Robert ; Willems, Lianne Irene ; King, Dustin T. ; Varghese, Vimal ; Britton, Robert ; Vocadlo, David J. ; Davies, Gideon John. / Structural and functional insight into human O-GlcNAcase. In: NATURE CHEMICAL BIOLOGY. 2017 ; Vol. 13, No. 6. pp. 610-612.

Bibtex - Download

@article{3f22d8c579c24cebad8bd4f18d83db9f,
title = "Structural and functional insight into human O-GlcNAcase",
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.",
keywords = "Acetylglucosamine/metabolism, Binding Sites, Enzyme Activation/drug effects, Enzyme Inhibitors/pharmacology, HEK293 Cells, Humans, Ligands, Models, Molecular, Protein Binding, Protein Isoforms/chemistry, Protein Structure, Tertiary, beta-N-Acetylhexosaminidases/chemistry",
author = "Christian Roth and Chan, {Oi Yi} and Offen, {Wendy Anne} and Hemsworth, {Glyn Robert} and Willems, {Lianne Irene} and King, {Dustin T.} and Vimal Varghese and Robert Britton and Vocadlo, {David J.} and Davies, {Gideon John}",
note = "{\textcopyright} 2017, Nature America, Inc. This is an author-produced version of the published paper. Uploaded in accordance with the publisher{\textquoteright}s self-archiving policy. Further copying may not be permitted; contact the publisher for details.",
year = "2017",
month = jun,
day = "1",
doi = "10.1038/nchembio.2358",
language = "English",
volume = "13",
pages = "610--612",
journal = "NATURE CHEMICAL BIOLOGY",
issn = "1552-4450",
publisher = "Nature Publishing Group",
number = "6",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Structural and functional insight into human O-GlcNAcase

AU - Roth, Christian

AU - Chan, Oi Yi

AU - Offen, Wendy Anne

AU - Hemsworth, Glyn Robert

AU - Willems, Lianne Irene

AU - King, Dustin T.

AU - Varghese, Vimal

AU - Britton, Robert

AU - Vocadlo, David J.

AU - Davies, Gideon John

N1 - © 2017, Nature America, Inc. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.

PY - 2017/6/1

Y1 - 2017/6/1

N2 - 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.

AB - 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.

KW - Acetylglucosamine/metabolism

KW - Binding Sites

KW - Enzyme Activation/drug effects

KW - Enzyme Inhibitors/pharmacology

KW - HEK293 Cells

KW - Humans

KW - Ligands

KW - Models, Molecular

KW - Protein Binding

KW - Protein Isoforms/chemistry

KW - Protein Structure, Tertiary

KW - beta-N-Acetylhexosaminidases/chemistry

UR - http://www.scopus.com/inward/record.url?scp=85016135486&partnerID=8YFLogxK

U2 - 10.1038/nchembio.2358

DO - 10.1038/nchembio.2358

M3 - Article

AN - SCOPUS:85016135486

VL - 13

SP - 610

EP - 612

JO - NATURE CHEMICAL BIOLOGY

JF - NATURE CHEMICAL BIOLOGY

SN - 1552-4450

IS - 6

ER -

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