O-GlcNAc transferase
From Proteopedia
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'''O-GlcNac transferase''' (OGT) catalyzes the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues by O-glycosylation. OGT contains 2 subunits: a 110 kDa and a 78kDa. The 110 kDa subunit contains a superhelical domain with 13 tetratricopeptide (TPR) repeats. The TPR motif consists of 34 amino acids and mediates protein-protein interactions. For details see [[Human O-GlcNAc transferase]]. | '''O-GlcNac transferase''' (OGT) catalyzes the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues by O-glycosylation. OGT contains 2 subunits: a 110 kDa and a 78kDa. The 110 kDa subunit contains a superhelical domain with 13 tetratricopeptide (TPR) repeats. The TPR motif consists of 34 amino acids and mediates protein-protein interactions. For details see [[Human O-GlcNAc transferase]]. | ||
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==3D structures of O-GlcNAc transferase== | ==3D structures of O-GlcNAc transferase== | ||
Revision as of 12:02, 8 February 2016
O-GlcNac transferase (OGT) catalyzes the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues by O-glycosylation. OGT contains 2 subunits: a 110 kDa and a 78kDa. The 110 kDa subunit contains a superhelical domain with 13 tetratricopeptide (TPR) repeats. The TPR motif consists of 34 amino acids and mediates protein-protein interactions. For details see Human O-GlcNAc transferase.
3D structures of O-GlcNAc transferase
Updated on 08-February-2016
