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Sci. STKE, 29 November 2005
[DOI: 10.1126/stke.3122005re13]

The Hexosamine Signaling Pathway: Deciphering the 'O-GlcNAc-Code'
(Rotating Molecule)

Dona C. Love and John A. Hanover*

Laboratory of Cell Biochemistry and Biology, NIDDK, NIH, Bethesda, MD 20892, USA

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*Corresponding author. E-mail, jah{at}helix.nih.gov

X-ray structure of the TPR domain of OGT and the basis of substrate recognition. The TPR domain of OGT forms a homodimer of right-handed super-helices. The dimer is maintained through mainly hydrophobic interactions. The concave surface of the super helix is lined with asparagine residues. Like the peptide-binding surface of importin alpha, this contiguous stretch of asparagines may allow OGT to interact with substrates. Click the image to the right to open a movie of a 360° rotation of the OGT homodimer about the homodimer interface.

Technical Details

Format: Movie file (mpg file)

Size: 4.9 MB

Requirements: This movie will play with Windows Media Player or other standard media players. (http://www.microsoft.com/windows/windowsmedia/default.aspx).

Citation: D. C. Love, J. A. Hanover, The hexosamine signaling pathway: Deciphering the "O-GlcNAc-Code". Sci. STKE 2005, re13 (2005).

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