About: Exploring the Reaction Mechanism of O-GlcNAc Transferase using QM/MM Molecular Dynamics

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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. (en)
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 (en)
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 (en)
skos:notation	RIV/00216224:14740/14:00079604!RIV15-MSM-14740___
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(LH13055)
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Kozmon, Stanislav Koča, Jaroslav Kumari, Manju
http://linked.open.../riv/druhVysledku	O - Ostatní výsledky nezařaditelné do žádného z výše uvedených druhů výsledku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Středoevropský technologický institut
http://linked.open...dnocenehoVysledku	16112
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/14:00079604
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	glycosyltransferase; QM/MM MD; reaction mechanism (en)
http://linked.open.../riv/klicoveSlovo	glycosyltransferase reaction mechanism QM/MM MD
http://linked.open...ontrolniKodProRIV	[EAAF4A8002A3]
http://linked.open...in/vavai/riv/obor	CF
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	4 (xsd:int)
http://linked.open...vavai/riv/projekt	Multidisciplinary Approach to Drug Design - Inhibition of Carbohydrate Acting Proteins
http://linked.open...UplatneniVysledku	2014
http://linked.open...iv/tvurceVysledku	Koča, Jaroslav Kozmon, Stanislav Tvaroška, Igor Kumari, Manju
http://localhost/t...ganizacniJednotka	14740

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