1v1h

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[[Image:1v1h.png|left|200px]]
 
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==Adenovirus fibre shaft sequence N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif with a short linker==
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The line below this paragraph, containing "STRUCTURE_1v1h", creates the "Structure Box" on the page.
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<StructureSection load='1v1h' size='340' side='right'caption='[[1v1h]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1v1h]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [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=1V1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V1H FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=1v1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v1h OCA], [https://pdbe.org/1v1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v1h RCSB], [https://www.ebi.ac.uk/pdbsum/1v1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v1h ProSAT]</span></td></tr>
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{{STRUCTURE_1v1h| PDB=1v1h | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/WAC_BPT4 WAC_BPT4] Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers').[https://www.uniprot.org/uniprot/SPIKE_ADE02 SPIKE_ADE02] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host coxsackievirus and adenovirus receptor CXADR located at the cell tight junctions to provide virion initial attachment to target cell. The fiber protein binds to CXADR with a higher affinity than CXADR binds to itself, thereby blocking the cell-cell adhesion function of CXADR dimers and leading to local disruption of the tight junction. Fiber protein present on neo-synthesized particles may thus disrupt the junctional integrity in order to facilitate further neighboring cells infection. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Fiber shedding is dependent on viral CXADR drifting motion and subsequent binding to immobile integrins. Heparan sulfate might also play a role in virus binding.<ref>PMID:10704346</ref> <ref>PMID:12297051</ref> <ref>PMID:21843868</ref> <ref>PMID:9525681</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/1v1h_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1v1h ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Adenovirus fibres are trimeric proteins that consist of a globular C-terminal domain, a central fibrous shaft and an N-terminal part that attaches to the viral capsid. In the presence of the globular C-terminal domain, which is necessary for correct trimerisation, the shaft segment adopts a triple beta-spiral conformation. We have replaced the head of the fibre by the trimerisation domain of the bacteriophage T4 fibritin, the foldon. Two different fusion constructs were made and crystallised, one with an eight amino acid residue linker and one with a linker of only two residues. X-ray crystallographic studies of both fusion proteins shows that residues 319-391 of the adenovirus type 2 fibre shaft fold into a triple beta-spiral fold indistinguishable from the native structure, although this is now resolved at a higher resolution of 1.9 A. The foldon residues 458-483 also adopt their natural structure. The intervening linkers are not well ordered in the crystal structures. This work shows that the shaft sequences retain their capacity to fold into their native beta-spiral fibrous fold when fused to a foreign C-terminal trimerisation motif. It provides a structural basis to artificially trimerise longer adenovirus shaft segments and segments from other trimeric beta-structured fibre proteins. Such artificial fibrous constructs, amenable to crystallisation and solution studies, can offer tractable model systems for the study of beta-fibrous structure. They can also prove useful for gene therapy and fibre engineering applications.
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===ADENOVIRUS FIBRE SHAFT SEQUENCE N-TERMINALLY FUSED TO THE BACTERIOPHAGE T4 FIBRITIN FOLDON TRIMERISATION MOTIF WITH A SHORT LINKER===
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Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif.,Papanikolopoulou K, Teixeira S, Belrhali H, Forsyth VT, Mitraki A, van Raaij MJ J Mol Biol. 2004 Sep 3;342(1):219-27. PMID:15313619<ref>PMID:15313619</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1v1h" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15313619}}, adds the Publication Abstract to the page
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*[[Fibritin|Fibritin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15313619 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15313619}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia virus T4]]
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[[1v1h]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_type_2,_bacteriophage_t4 Human adenovirus type 2, bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V1H OCA].
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[[Category: Human adenovirus 2]]
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[[Category: Large Structures]]
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==Reference==
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[[Category: Belrhali H]]
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<ref group="xtra">PMID:15313619</ref><ref group="xtra">PMID:14699113</ref><ref group="xtra">PMID:10553913</ref><ref group="xtra">PMID:9757094</ref><references group="xtra"/>
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[[Category: Forsyth VT]]
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[[Category: Human adenovirus type 2, bacteriophage t4]]
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[[Category: Mitraki A]]
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[[Category: Belrhali, H.]]
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[[Category: Papanikolopoulou K]]
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[[Category: Forsyth, V T.]]
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[[Category: Teixeira S]]
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[[Category: Mitraki, A.]]
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[[Category: Van Raaij MJ]]
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[[Category: Papanikolopoulou, K.]]
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[[Category: Raaij, M J.Van.]]
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[[Category: Teixeira, S.]]
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[[Category: Adenovirus]]
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[[Category: Chimera]]
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[[Category: Fiber protein]]
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Current revision

Adenovirus fibre shaft sequence N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif with a short linker

PDB ID 1v1h

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