1x9t: Difference between revisions

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{{Seed}}
[[Image:1x9t.png|left|200px]]


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==The crystal structure of human adenovirus 2 penton base in complex with an ad2 N-terminal fibre peptide==
The line below this paragraph, containing "STRUCTURE_1x9t", creates the "Structure Box" on the page.
<StructureSection load='1x9t' size='340' side='right'caption='[[1x9t]], [[Resolution|resolution]] 3.50&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'>[[1x9t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_adenovirus_2 Human adenovirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X9T 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]] 3.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C15:N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE'>C15</scene></td></tr>
{{STRUCTURE_1x9t| PDB=1x9t |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1x9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9t OCA], [https://pdbe.org/1x9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x9t RCSB], [https://www.ebi.ac.uk/pdbsum/1x9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x9t ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAPSP_ADE02 CAPSP_ADE02] Major capsid protein that self-associates to form penton base pentamers, each in the shape of a pentagon, situated at the 12 vertices of the pseudo T=25 capsid. Involved in virus secondary attachment to host cell after initial attachment by the fiber protein. Binds host integrin heterodimer ITGAV-ITGB5 (alphaV-beta5) thereby triggering clathrin-mediated endocytosis of virions. Mediates initial virus attachment to CXADR-negative cells. Binding to integrins ITGAV-ITGB5 also seems to induce macropinocytosis uptake of the virus. As the virus enters the host cell, penton proteins are shed concomitant with virion acidification in the endosome.<ref>PMID:12221069</ref> <ref>PMID:20615244</ref> <ref>PMID:20798312</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/x9/1x9t_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=1x9t ConSurf].
<div style="clear:both"></div>


===The crystal structure of human adenovirus 2 penton base in complex with an ad2 N-terminal fibre peptide===
==See Also==
 
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 
== References ==
<!--
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{{ABSTRACT_PUBMED_15629723}}
 
==About this Structure==
1X9T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_2 Human adenovirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9T OCA].
 
==Reference==
The structure of the human adenovirus 2 penton., Zubieta C, Schoehn G, Chroboczek J, Cusack S, Mol Cell. 2005 Jan 7;17(1):121-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15629723 15629723]
[[Category: Human adenovirus 2]]
[[Category: Human adenovirus 2]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chroboczek, J.]]
[[Category: Chroboczek J]]
[[Category: Cusack, S.]]
[[Category: Cusack S]]
[[Category: Schoehn, G.]]
[[Category: Schoehn G]]
[[Category: Zubieta, C.]]
[[Category: Zubieta C]]
[[Category: Anti-parallel beta sheet]]
[[Category: Insertion domain]]
[[Category: Jellyroll domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:08:42 2008''

Latest revision as of 16:36, 13 March 2024

The crystal structure of human adenovirus 2 penton base in complex with an ad2 N-terminal fibre peptideThe crystal structure of human adenovirus 2 penton base in complex with an ad2 N-terminal fibre peptide

Structural highlights

1x9t is a 2 chain structure with sequence from Human adenovirus 2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAPSP_ADE02 Major capsid protein that self-associates to form penton base pentamers, each in the shape of a pentagon, situated at the 12 vertices of the pseudo T=25 capsid. Involved in virus secondary attachment to host cell after initial attachment by the fiber protein. Binds host integrin heterodimer ITGAV-ITGB5 (alphaV-beta5) thereby triggering clathrin-mediated endocytosis of virions. Mediates initial virus attachment to CXADR-negative cells. Binding to integrins ITGAV-ITGB5 also seems to induce macropinocytosis uptake of the virus. As the virus enters the host cell, penton proteins are shed concomitant with virion acidification in the endosome.[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. ↑ Meier O, Boucke K, Hammer SV, Keller S, Stidwill RP, Hemmi S, Greber UF. Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake. J Cell Biol. 2002 Sep 16;158(6):1119-31. Epub 2002 Sep 9. PMID:12221069 doi:http://dx.doi.org/10.1083/jcb.200112067
  2. ↑ Lyle C, McCormick F. Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-negative cells. Virol J. 2010 Jul 8;7:148. doi: 10.1186/1743-422X-7-148. PMID:20615244 doi:10.1186/1743-422X-7-148
  3. ↑ Liu H, Jin L, Koh SB, Atanasov I, Schein S, Wu L, Zhou ZH. Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science. 2010 Aug 27;329(5995):1038-43. PMID:20798312 doi:10.1126/science.1187433

1x9t, resolution 3.50Å

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