Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 15, Issue 7, Pages 764-765Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1443
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Funding
- Biotechnology and Biological Sciences Research Council [BB/F007124/1] Funding Source: researchfish
- BBSRC [BB/F007124/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F007124/1] Funding Source: Medline
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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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