Title : Structural insights into mechanism and specificity of O-GlcNAc transferase.

Pub. Date : 2008 Oct 22

PMID : 18818698






1 Functional Relationships(s)
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1 Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop. Metals O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens