| Literature DB >> 18536723 |
Carlos Martinez-Fleites1, Matthew S Macauley, Yuan He, David L Shen, David J Vocadlo, Gideon J Davies.
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.Entities:
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Year: 2008 PMID: 18536723 DOI: 10.1038/nsmb.1443
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369