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[[Image:1dto.gif|left|200px]]


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==CRYSTAL STRUCTURE OF THE COMPLETE TRANSACTIVATION DOMAIN OF E2 PROTEIN FROM THE HUMAN PAPILLOMAVIRUS TYPE 16==
The line below this paragraph, containing "STRUCTURE_1dto", creates the "Structure Box" on the page.
<StructureSection load='1dto' size='340' side='right'caption='[[1dto]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1dto]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_papillomavirus_type_16 Human papillomavirus type 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DTO FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dto OCA], [https://pdbe.org/1dto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dto RCSB], [https://www.ebi.ac.uk/pdbsum/1dto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dto ProSAT]</span></td></tr>
{{STRUCTURE_1dto| PDB=1dto |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/VE2_HPV16 VE2_HPV16] Plays an accessory role in initiation of DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.<ref>PMID:3033289</ref> <ref>PMID:1326651</ref> <ref>PMID:15681049</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dt/1dto_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=1dto ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF THE COMPLETE TRANSACTIVATION DOMAIN OF E2 PROTEIN FROM THE HUMAN PAPILLOMAVIRUS TYPE 16'''
==See Also==
 
*[[Regulatory protein E2|Regulatory protein E2]]
 
== References ==
==Overview==
<references/>
Papillomaviruses cause warts and proliferative lesions in skin and other epithelia. In a minority of papillomavirus types ('high risk, including human papillomaviruses 16, 18, 31, 33, 45 and 56), further transformation of the wart lesions can produce tumours. The papillomavirus E2 protein controls primary transcription and replication of the viral genome. Both activities are governed by a approximately 200 amino-acid amino-terminal module (E2NT) which is connected to a DNA-binding carboxy-terminal module by a flexible linker. Here we describe the crystal structure of the complete E2NT module from human papillomavirus 16. The E2NT module forms a dimer both in the crystal and in solution. Amino acids that are necessary for transactivation are located at the dimer interface, indicating that the dimer structure may be important in the interactions of E2NT with viral and cellular transcription factors. We propose that dimer formation may contribute to the stabilization of DNA loops which may serve to relocate distal DNA-binding transcription factors to the site of human papillomavirus transcription initiation.
__TOC__
 
</StructureSection>
==About this Structure==
1DTO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_papillomavirus_type_16 Human papillomavirus type 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTO OCA].
 
==Reference==
Structure of the intact transactivation domain of the human papillomavirus E2 protein., Antson AA, Burns JE, Moroz OV, Scott DJ, Sanders CM, Bronstein IB, Dodson GG, Wilson KS, Maitland NJ, Nature. 2000 Feb 17;403(6771):805-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10693813 10693813]
[[Category: Human papillomavirus type 16]]
[[Category: Human papillomavirus type 16]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Antson, A A.]]
[[Category: Antson AA]]
[[Category: Bronstein, I B.]]
[[Category: Bronstein IB]]
[[Category: Burns, J E.]]
[[Category: Burns JE]]
[[Category: Dodson, G G.]]
[[Category: Dodson GG]]
[[Category: Maitland, N.]]
[[Category: Maitland N]]
[[Category: Moroz, O V.]]
[[Category: Moroz OV]]
[[Category: Sanders, C M.]]
[[Category: Sanders CM]]
[[Category: Scott, D J.]]
[[Category: Scott DJ]]
[[Category: Wilson, K S.]]
[[Category: Wilson KS]]
[[Category: Beta-sheet]]
[[Category: Three-helix bundle]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:15:42 2008''

Latest revision as of 09:59, 7 February 2024

CRYSTAL STRUCTURE OF THE COMPLETE TRANSACTIVATION DOMAIN OF E2 PROTEIN FROM THE HUMAN PAPILLOMAVIRUS TYPE 16CRYSTAL STRUCTURE OF THE COMPLETE TRANSACTIVATION DOMAIN OF E2 PROTEIN FROM THE HUMAN PAPILLOMAVIRUS TYPE 16

Structural highlights

1dto is a 1 chain structure with sequence from Human papillomavirus type 16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VE2_HPV16 Plays an accessory role in initiation of DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Phelps WC, Howley PM. Transcriptional trans-activation by the human papillomavirus type 16 E2 gene product. J Virol. 1987 May;61(5):1630-8. PMID:3033289
  2. ↑ Del Vecchio AM, Romanczuk H, Howley PM, Baker CC. Transient replication of human papillomavirus DNAs. J Virol. 1992 Oct;66(10):5949-58. PMID:1326651
  3. ↑ Okoye A, Cordano P, Taylor ER, Morgan IM, Everett R, Campo MS. Human papillomavirus 16 L2 inhibits the transcriptional activation function, but not the DNA replication function, of HPV-16 E2. Virus Res. 2005 Mar;108(1-2):1-14. PMID:15681049 doi:10.1016/j.virusres.2004.07.004

1dto, resolution 1.90Å

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