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Three-dimensional homology model of GlcNAc-TV glycosyltransferase.

Abstract：

:The enzyme UDP-N-acetylglucosamine: α-d-mannoside β-1-6 N-acetylglucosaminyltransferase V (GnT-V) catalyzes the transfer of GlcNAc from the UDP-GlcNAc donor to the α-1-6-linked mannose of the trimannosyl core structure of glycoproteins to produce the β-1-6-linked branching of N-linked oligosaccharides. β-1-6-GlcNAc-branched N-glycans are associated with cancer growth and metastasis. Therefore, the inhibition of GnT-V represents a key target for anti-cancer drug development. However, the development of potent and specific inhibitors of GnT-V is hampered by the lack of information on the three-dimensional structure of the enzyme and on the binding characteristics of its substrates. Here we present the first 3D structure of GnT-V as a result of homology modeling. Various alignment methods, docking the donor and acceptor substrates, and molecular dynamics simulation were used to construct seven homology models of GnT-V and characterize the binding of its substrates. The best homology model is consistent with available experimental data. The three-dimensional model, the structure of the enzyme catalytic site and binding information obtained for the donor and acceptor can be useful in studies of the catalytic mechanism and design of inhibitors of GnT-V.

journal_name

Glycobiology

journal_title

Glycobiology

authors

Janoš P,Kozmon S,Tvaroška I,Koca J

doi

10.1093/glycob/cww010

subject

Has Abstract

pub_date

2016-07-01 00:00:00

pages

757-771

issue

7

eissn

0959-6658

issn

1460-2423

pii

cww010

journal_volume

26

pub_type

杂志文章

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