Defining the structural origin of the substrate sequence independence of O-GlcNAcase using a combination of molecular docking and dynamics simulation

Glycobiology

Volumn 24, Issue 1, 2014, Pages 85-96

  Martin, Joanne C ^a   Fadda, Elisa ^a   Ito, Keigo ^b   Woods, Robert J ^a,b  

^a NATIONAL UNIVERSITY OF IRELAND   (Ireland)

^b UNIVERSITY OF GEORGIA   (United States)

Author keywords

N Acetylglucosaminidase (O GlcNAcase); GLYCAM; Molecular dynamics; O Linked N acetyl glucosamine (O GlcNAc); Protein glycosylation

Indexed keywords

ACETYLGLUCOSAMINIDASE; ALANINE; BACTERIAL ENZYME; GLYCOPEPTIDE; HISTONE H3; MYC PROTEIN; N ACETYLGLUCOSAMINE; POLYPEPTIDE; PROTEIN P53;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; ENZYME KINETICS; ENZYME STRUCTURE; HYDROGEN BOND; MOLECULAR DOCKING; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CARBOHYDRATE INTERACTION; PROTEIN CONFORMATION; PROTEIN STABILITY;

GLYCAM; MOLECULAR DYNAMICS; O-LINKED N-ACETYL-GLUCOSAMINE (O-GLCNAC); PROTEIN GLYCOSYLATION; Β-N-ACETYLGLUCOSAMINIDASE (O-GLCNACASE);

BACTERIAL PROTEINS; BACTEROIDES; BETA-N-ACETYLHEXOSAMINIDASES; ENZYME INHIBITORS; MOLECULAR DOCKING SIMULATION; MOLECULAR DYNAMICS SIMULATION; SEQUENCE ANALYSIS, PROTEIN;

EID: 84890424846     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwt094     Document Type: Article

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