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2BOP

CRYSTAL STRUCTURE AT 1.7 ANGSTROMS OF THE BOVINE PAPILLOMAVIRUS-1 E2 DNA-BINDING DOMAIN BOUND TO ITS DNA TARGET

Summary for 2BOP
Entry DOI10.2210/pdb2bop/pdb
DescriptorDNA (5'-D(*CP*CP*GP*AP*CP*CP*GP*AP*CP*GP*TP*CP*GP*GP*TP*CP*G )-3'), PROTEIN (E2), YTTERBIUM (III) ION, ... (4 entities in total)
Functional Keywordsprotein-dna complex, double helix, transcription-dna complex, transcription/dna
Biological sourceBovine papillomavirus type 1
Total number of polymer chains2
Total formula weight15156.32
Authors
Hegde, R.S.,Grossman, S.R.,Laimins, L.A.,Sigler, P.B. (deposition date: 1994-01-13, release date: 1994-01-31, Last modification date: 2024-02-14)
Primary citationHegde, R.S.,Grossman, S.R.,Laimins, L.A.,Sigler, P.B.
Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target.
Nature, 359:505-512, 1992
Cited by
PubMed Abstract: The dominant transcriptional regulator of the papillomaviruses, E2, binds to its specific DNA target through a previously unobserved dimeric antiparallel beta-barrel. The DNA is severely but smoothly bent over the barrel by the interaction of successive major grooves with a pair of symmetrically disposed alpha-helices. The specific interface is an 'interwoven' network of interactions where the identifying base pairs of the target contact more than one amino-acid side chain and the discriminating amino acids interact with more than one base pair.
PubMed: 1328886
DOI: 10.1038/359505a0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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