Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation.,Martinez-Fleites C, Macauley MS, He Y, Shen DL, Vocadlo DJ, Davies GJ Nat Struct Mol Biol. 2008 Jul;15(7):764-5. Epub 2008 Jun 8. PMID:18536723[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martinez-Fleites C, Macauley MS, He Y, Shen DL, Vocadlo DJ, Davies GJ. Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. Nat Struct Mol Biol. 2008 Jul;15(7):764-5. Epub 2008 Jun 8. PMID:18536723 doi:nsmb.1443
