Docking study of the potential glycosyltransferase inhibitors
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F09%3A00039161" target="_blank" >RIV/00216224:14310/09:00039161 - isvavai.cz</a>
Result on the web
—
DOI - Digital Object Identifier
—
Alternative languages
Result language
angličtina
Original language name
Docking study of the potential glycosyltransferase inhibitors
Original language description
Glycosyltransferases are involved in the biosynthesis of glycans, which play an important role in many biological events. The N-acetylglucosaminyltransferase I catalyzes the transfer of a GlcNAc residue from the donor UDP-GlcNAc to the acceptor, which isthe C2-hydroxyl group of a mannose residue in the trimannosyl core of the Man5GlcNAc2-Asn-X oligosaccharide. Previous molecular modeling studies determined the structure of a transition state (TS) for the enzymatic reaction catalyzed by GnT-I. The proposed scaffold uses the alkylthio and phosphonate groups linked to the anomeric centre of five-member ring to mimic the arrangement of GlcNAc, UDP and acceptor in TS. The conformational properties of the analogue were investigated by DFT(B3LYP) methods using Schrödinger software packages. a- and b- anomers of the stable conformer were docked into crystal structure of GnT-I (PDB code 1FOA) using the Glide software. The binding energy was computed using the Liaison software.
Czech name
—
Czech description
—
Classification
Type
O - Miscellaneous
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
—
Result continuities
Project
—
Continuities
S - Specificky vyzkum na vysokych skolach
Others
Publication year
2009
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů