2c62 | pdb_00002c62
From Proteopedia
CRYSTAL STRUCTURE OF THE HUMAN TRANSCRIPTION COFACTOR PC4 IN COMPLEX WITH SINGLE-STRANDED DNA
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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
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This page was last modified 17:22, 15 January 2015.