1x9p: Difference between revisions

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OCA

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-[[Image:1x9p.gif|left|200px]]<br /><applet load="1x9p" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1x9p, resolution 3.30&Aring;" />
-'''The crystal structure of human adenovirus 2 penton base'''<br />
-==Overview==
+==The crystal structure of human adenovirus 2 penton base==
-The adenovirus penton, a noncovalent complex of the pentameric penton base, and trimeric fiber proteins, comprises the vertices of the adenovirus, capsid and contains all necessary components for viral attachment and, internalization. The 3.3 A resolution crystal structure of human, adenovirus 2 (hAd2) penton base shows that the monomer has a basal, jellyroll domain and a distal irregular domain formed by two long, insertions, a similar topology to the adenovirus hexon. The Arg-Gly-Asp, (RGD) motif, required for interactions with cellular integrins, occurs on, a flexible surface loop. The complex of penton base with bound N-terminal, fiber peptide, determined at 3.5 A resolution, shows that the universal, fiber motif FNPVYPY binds at the interface of adjacent penton base, monomers and results in a localized structural rearrangement in the, insertion domain of the penton base. These results give insight into the, structure and assembly of the adenovirus capsid and will be of use for, gene-therapy applications.
+<StructureSection load='1x9p' size='340' side='right'caption='[[1x9p]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1x9p]] is a 1 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=1X9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X9P FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
+<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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1x9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9p OCA], [https://pdbe.org/1x9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x9p RCSB], [https://www.ebi.ac.uk/pdbsum/1x9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x9p 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/x9/1x9p_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=1x9p ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-X9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_2 Human adenovirus 2] with SO4 and C15 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X9P OCA].
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
+== References ==
-==Reference==
+<references/>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15629723 15629723]
+__TOC__
+</StructureSection>
 [[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: C15]]
-[[Category: SO4]]
-[[Category: anti-parallel beta sheet]]
-[[Category: insertion domain]]
-[[Category: jellyroll domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:55:13 2007''