Sandbox Reserved 381: Difference between revisions
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Sheri Marcum (talk | contribs) /* Your Heading Here (maybe something like 'Structure')==<StructureSection load='1w3b' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry 1w3b)' scene=''>Anything in this section will appear adjacent to the 3D structure an |
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O-GlcNAc modification has been described for a large and still increasing number of proteins, many of which are key modulators of cellular signalling. O-GlcNAc modifications are catalysed by a glycosyltransferase named O-linked N-acetylglucosaminyltranserase (OGT), and are removed by the antagonistic enzyme B-N-acetylglucosaminidase (O-GlcNAcase). The general scheme of O-linked N-acetylglucosamine modification suggests that N-acetylglucosamine is added to serine/threonine (Ser/Thr) residues of target proteins by the enzyme OGT using UDP-GlcNac as substrate. The N-acetylglucosamine group is removed by the antagonistic activity of O-GlcNAcase. <ref>Alexander G, Danilo G. The O-linked N-acetylglucosamine modification in cellular signalling and the immune system. EMBO reports. 2008 June;9:748-753[http://www.nature.com/embor/journal/v9/n8/full/embor2008129.html]</ref> | O-GlcNAc modification has been described for a large and still increasing number of proteins, many of which are key modulators of cellular signalling. O-GlcNAc modifications are catalysed by a glycosyltransferase named O-linked N-acetylglucosaminyltranserase (OGT), and are removed by the antagonistic enzyme B-N-acetylglucosaminidase (O-GlcNAcase). The general scheme of O-linked N-acetylglucosamine modification suggests that N-acetylglucosamine is added to serine/threonine (Ser/Thr) residues of target proteins by the enzyme OGT using UDP-GlcNac as substrate. The N-acetylglucosamine group is removed by the antagonistic activity of O-GlcNAcase. <ref>Alexander G, Danilo G. The O-linked N-acetylglucosamine modification in cellular signalling and the immune system. EMBO reports. 2008 June;9:748-753[http://www.nature.com/embor/journal/v9/n8/full/embor2008129.html]</ref> | ||
== N Terminus == | |||
The N terminus of OGT is unusual, consisting of 2.5-13.5 tetratricopeptide repeats (TPRs) dpending on alternative splicing.<ref>Kreppel L, Hart G. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem. 1999;274:32015-32022</ref> | The N terminus of OGT is unusual, consisting of 2.5-13.5 tetratricopeptide repeats (TPRs) dpending on alternative splicing.<ref>Kreppel L, Hart G. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem. 1999;274:32015-32022</ref> | ||
Your Heading Here (maybe something like 'Structure')==<StructureSection load='1w3b' size='200' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1w3b]])' scene=''>Anything in this section will appear adjacent to the 3D structure and will be scrollable.</StructureSection> | |||
== Tetanospasmin (TeNT) == | == Tetanospasmin (TeNT) == | ||
