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
The 1.74-A crystal structure of the human transcription cofactor PC4 in complex with a single-stranded 20-mer oligonucleotide reveals how symmetry-related beta-surfaces of the protein homodimer interact with juxtaposed 5-nucleotide DNA regions running in opposite directions. The structure explains high-affinity binding of PC4 to the complementary strands of unwinding duplex DNA, and it suggests the cofactor may have a role in relaxing negative supercoils or exposing unpaired bases for sequence-specific recognition by other biomolecules.
A global transcription cofactor bound to juxtaposed strands of unwound DNA.,Werten S, Moras D Nat Struct Mol Biol. 2006 Feb;13(2):181-2. Epub 2006 Jan 15. PMID:16415882[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Werten S, Moras D. A global transcription cofactor bound to juxtaposed strands of unwound DNA. Nat Struct Mol Biol. 2006 Feb;13(2):181-2. Epub 2006 Jan 15. PMID:16415882 doi:10.1038/nsmb1044
