1dch: Difference between revisions

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[[Image:1dch.gif|left|200px]]
{{Seed}}
[[Image:1dch.png|left|200px]]


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{{STRUCTURE_1dch|  PDB=1dch  |  SCENE=  }}  
{{STRUCTURE_1dch|  PDB=1dch  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR'''
===CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_7725101}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_7725101}}


==About this Structure==
==About this Structure==
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[[Category: Transcriptional simulator]]
[[Category: Transcriptional simulator]]
[[Category: Transregulator of homeodomain protein]]
[[Category: Transregulator of homeodomain protein]]
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