1qqh

<StructureSection load='1qqh' size='340' side='right' caption='[[1qqh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[1qqh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hpv18 Hpv18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QQH FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qqh OCA], [http://pdbe.org/1qqh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qqh RCSB], [http://www.ebi.ac.uk/pdbsum/1qqh PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/VE2_HPV18 VE2_HPV18]] E2 regulates viral transcription and DNA replication. It binds to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory region. It can either activate or repress transcription depending on E2RE's position with regards to proximal promoter elements. Repression occurs by sterically hindering the assembly of the transcription initiation complex. The E1-E2 complex binds to the origin of DNA replication.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qq/1qqh_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The papillomavirus E2 protein regulates viral transcription and DNA replication through interactions with cellular and viral proteins. The amino-terminal activation domain, which represents a protein class whose structural themes are poorly understood, contains key residues that mediate these functional contacts. The crystal structure of a protease-resistant core of the human papillomavirus type 18 E2 activation domain reveals a novel fold creating a cashew-shaped form with a glutamine-rich alpha helix packed against a beta-sheet framework. The protein surface shows extensive overlap of determinants for replication and transcription. The structure broadens the concept of activators to include proteins with potentially malleable, but certainly ordered, structures.

Crystal structure of the human papillomavirus type 18 E2 activation domain.,Harris SF, Botchan MR Science. 1999 Jun 4;284(5420):1673-7. PMID:10356398<ref>PMID:10356398</ref>

== References ==

[[Category: Hpv18]]

[[Category: Botchan, M R]]

[[Category: Harris, S F]]

[[Category: Amphipathic helix]]

[[Category: Viral protein]]