Three-dimensional homology model of GlcNAc-TV glycosyltransferase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F16%3A00089828" target="_blank" >RIV/00216224:14310/16:00089828 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1093/glycob/cww010" target="_blank" >http://dx.doi.org/10.1093/glycob/cww010</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/glycob/cww010" target="_blank" >10.1093/glycob/cww010</a>
Alternative languages
Result language
angličtina
Original language name
Three-dimensional homology model of GlcNAc-TV glycosyltransferase
Original language description
The enzyme UDP-N-acetylglucosamine: a-d-mannoside b-1-6 N-acetylglucosaminyltransferase V (GnT-V) catalyzes the transfer of GlcNAc from the UDP-GlcNAc donor to the a-1-6-linked mannose of the trimannosyl core structure of glycoproteins to produce the b-1-6-linked branching of N-linked oligosaccharides. b-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.
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Glycobiology
ISSN
0959-6658
e-ISSN
—
Volume of the periodical
26
Issue of the periodical within the volume
7
Country of publishing house
US - UNITED STATES
Number of pages
15
Pages from-to
757-771
UT code for WoS article
000384766000009
EID of the result in the Scopus database
—