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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator.

DCoH, the dimerization cofactor of hepatocyte nuclear factor-1, stimulates gene expression by associating with specific DNA binding proteins and also catalyzes the dehydration of the biopterin cofactor of phenylalanine hydroxylase. The x-ray crystal structure determined at 3 angstrom resolution reveals that DCoH forms a tetramer containing two saddle-shaped grooves that comprise likely macromolecule binding sites. Two equivalent enzyme active sites flank each saddle, suggesting that there is a spatial connection between the catalytic and binding activities. Structural similarities between the DCoH fold and nucleic acid-binding proteins argue that the saddle motif has evolved to bind diverse ligands or that DCoH unexpectedly may bind nucleic acids.[1]


  1. Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator. Endrizzi, J.A., Cronk, J.D., Wang, W., Crabtree, G.R., Alber, T. Science (1995) [Pubmed]
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