Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator.,Endrizzi JA, Cronk JD, Wang W, Crabtree GR, Alber T Science. 1995 Apr 28;268(5210):556-9. PMID:7725101[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Endrizzi JA, Cronk JD, Wang W, Crabtree GR, Alber T. Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator. Science. 1995 Apr 28;268(5210):556-9. PMID:7725101
