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Statements

Subject Item
n2:RIV%2F00216224%3A14740%2F14%3A00079604%21RIV15-MSM-14740___
rdf:type
n9:Vysledek skos:Concept
dcterms:description
Glycosylation is one of the important post-translational modifications that provide greater proteomic diversity This event is also critical for a wide range of biological processes, such as cell adhesion, defense mechanism, cell proliferation, cancer metastasis etc through variety of glycoconjugates. These glycoconjugates are formed by glycosyltransferases which add saccharides onto proteins, lipids sugars etc. Here we are exploring the reaction mechanisms of O-GlcNAc transferase (OGTs), where GlcNAc is transferred to –OH group of Ser/Thr of the proteins. Three groups have proposed mechanisms on different crystal structures of OGTs, suggesting different catalytic base to abstract proton from Ser, 1) His498[1], 2) alpha-phosphate[2], and 3) water molecule shunting[3] , but still the process is not clear. In presented study we were trying to confirm one of the proposed mechanisms employing hybrid QM/MM CPMD molecular dynamics. We have modelled all three proposed mechanisms. Glycosylation is one of the important post-translational modifications that provide greater proteomic diversity This event is also critical for a wide range of biological processes, such as cell adhesion, defense mechanism, cell proliferation, cancer metastasis etc through variety of glycoconjugates. These glycoconjugates are formed by glycosyltransferases which add saccharides onto proteins, lipids sugars etc. Here we are exploring the reaction mechanisms of O-GlcNAc transferase (OGTs), where GlcNAc is transferred to –OH group of Ser/Thr of the proteins. Three groups have proposed mechanisms on different crystal structures of OGTs, suggesting different catalytic base to abstract proton from Ser, 1) His498[1], 2) alpha-phosphate[2], and 3) water molecule shunting[3] , but still the process is not clear. In presented study we were trying to confirm one of the proposed mechanisms employing hybrid QM/MM CPMD molecular dynamics. We have modelled all three proposed mechanisms.
dcterms:title
Exploring the Reaction Mechanism of O-GlcNAc Transferase using QM/MM Molecular Dynamics Exploring the Reaction Mechanism of O-GlcNAc Transferase using QM/MM Molecular Dynamics
skos:prefLabel
Exploring the Reaction Mechanism of O-GlcNAc Transferase using QM/MM Molecular Dynamics Exploring the Reaction Mechanism of O-GlcNAc Transferase using QM/MM Molecular Dynamics
skos:notation
RIV/00216224:14740/14:00079604!RIV15-MSM-14740___
n3:aktivita
n10:P
n3:aktivity
P(LH13055)
n3:dodaniDat
n17:2015
n3:domaciTvurceVysledku
n11:8988250 n11:4347374 Kumari, Manju
n3:druhVysledku
n13:O
n3:duvernostUdaju
n15:S
n3:entitaPredkladatele
n8:predkladatel
n3:idSjednocenehoVysledku
16112
n3:idVysledku
RIV/00216224:14740/14:00079604
n3:jazykVysledku
n14:eng
n3:klicovaSlova
glycosyltransferase; QM/MM MD; reaction mechanism
n3:klicoveSlovo
n5:reaction%20mechanism n5:glycosyltransferase n5:QM%2FMM%20MD
n3:kontrolniKodProRIV
[EAAF4A8002A3]
n3:obor
n7:CF
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
4
n3:projekt
n16:LH13055
n3:rokUplatneniVysledku
n17:2014
n3:tvurceVysledku
Kumari, Manju Kozmon, Stanislav Koča, Jaroslav Tvaroška, Igor
n4:organizacniJednotka
14740