Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation
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| Authors: | Martinez-Fleites, C; Macauley, MS; He, Y; Shen, DL; Vocadlo, DJ; Davies, GJ |
| Year: | 2008 |
| Journal: | Nat. Struct. Mol. Biol. 15: 764-765 Article Link (DOI) PubMed |
| Title: | Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation |
| Abstract: | N-Acetylglucosamine (O-GlcNAc) modification of proteins provides a mechanism for the control of diverse cellular processes through a dynamic interplay with phosphorylation. UDP-GlcNAc:polypeptidyl transferase (OGT) catalyzes O-GlcNAc addition. The structure of an intact OGT homolog and kinetic analysis of human OGT variants reveal a contiguous superhelical groove that directs substrates to the active site. |
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