This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2bop
From Proteopedia
|
CRYSTAL STRUCTURE AT 1.7 ANGSTROMS OF THE BOVINE PAPILLOMAVIRUS-1 E2 DNA-BINDING DOMAIN BOUND TO ITS DNA TARGET
Overview
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.
About this Structure
2BOP is a Single protein structure of sequence from Bovine papillomavirus type 1 with YB as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target., Hegde RS, Grossman SR, Laimins LA, Sigler PB, Nature. 1992 Oct 8;359(6395):505-12. PMID:1328886
Page seeded by OCA on Wed Nov 21 08:51:27 2007
