Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V

The activity of glycosyltransferase GnT-V correlates with cancer malignancy and poor prognosis but its mechanism of action is poorly understood. Here, the authors solve crystal structures of free and substrate analog-bound GnT-V, providing insights into its catalytic mechanism and a basis for GnT-V...

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Main Authors: Masamichi Nagae, Yasuhiko Kizuka, Emiko Mihara, Yu Kitago, Shinya Hanashima, Yukishige Ito, Junichi Takagi, Naoyuki Taniguchi, Yoshiki Yamaguchi
Format: Article
Language:English
Published: Nature Publishing Group 2018-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-05931-w
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spelling doaj-f1b4c8dd92254367b426de0599de41f52021-05-11T10:03:57ZengNature Publishing GroupNature Communications2041-17232018-08-019111210.1038/s41467-018-05931-wStructure and mechanism of cancer-associated N-acetylglucosaminyltransferase-VMasamichi Nagae0Yasuhiko Kizuka1Emiko Mihara2Yu Kitago3Shinya Hanashima4Yukishige Ito5Junichi Takagi6Naoyuki Taniguchi7Yoshiki Yamaguchi8Structural Glycobiology Team, Glycobiology Research Group, Global Research Cluster, RIKENDisease Glycomics Team, Systems Glycobiology Research Group, Global Research Cluster, RIKENInstitute for Protein Research, Osaka UniversityInstitute for Protein Research, Osaka UniversityDepartment of Chemistry, Osaka UniversitySynthetic Cellular Chemistry Laboratory, RIKENInstitute for Protein Research, Osaka UniversityDisease Glycomics Team, Systems Glycobiology Research Group, Global Research Cluster, RIKENStructural Glycobiology Team, Glycobiology Research Group, Global Research Cluster, RIKENThe activity of glycosyltransferase GnT-V correlates with cancer malignancy and poor prognosis but its mechanism of action is poorly understood. Here, the authors solve crystal structures of free and substrate analog-bound GnT-V, providing insights into its catalytic mechanism and a basis for GnT-V inhibition.https://doi.org/10.1038/s41467-018-05931-w
collection DOAJ
language English
format Article
sources DOAJ
author Masamichi Nagae
Yasuhiko Kizuka
Emiko Mihara
Yu Kitago
Shinya Hanashima
Yukishige Ito
Junichi Takagi
Naoyuki Taniguchi
Yoshiki Yamaguchi
spellingShingle Masamichi Nagae
Yasuhiko Kizuka
Emiko Mihara
Yu Kitago
Shinya Hanashima
Yukishige Ito
Junichi Takagi
Naoyuki Taniguchi
Yoshiki Yamaguchi
Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V
Nature Communications
author_facet Masamichi Nagae
Yasuhiko Kizuka
Emiko Mihara
Yu Kitago
Shinya Hanashima
Yukishige Ito
Junichi Takagi
Naoyuki Taniguchi
Yoshiki Yamaguchi
author_sort Masamichi Nagae
title Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V
title_short Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V
title_full Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V
title_fullStr Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V
title_full_unstemmed Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V
title_sort structure and mechanism of cancer-associated n-acetylglucosaminyltransferase-v
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2018-08-01
description The activity of glycosyltransferase GnT-V correlates with cancer malignancy and poor prognosis but its mechanism of action is poorly understood. Here, the authors solve crystal structures of free and substrate analog-bound GnT-V, providing insights into its catalytic mechanism and a basis for GnT-V inhibition.
url https://doi.org/10.1038/s41467-018-05931-w
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