2bop

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(New page: 200px<br /><applet load="2bop" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bop, resolution 1.700&Aring;" /> '''CRYSTAL STRUCTURE A...)
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Revision as of 06:44, 21 November 2007


2bop, resolution 1.700Å

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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

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