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New page: left|200px<br /><applet load="1nob" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nob, resolution 2.6Å" /> '''KNOB DOMAIN FROM ADEN... |
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== | ==KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12== | ||
Binding of virus particles to specific host cell surface receptors is | <StructureSection load='1nob' size='340' side='right'caption='[[1nob]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1nob]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_adenovirus_12 Human adenovirus 12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NOB 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]] 2.6Å</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=1nob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nob OCA], [https://pdbe.org/1nob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nob RCSB], [https://www.ebi.ac.uk/pdbsum/1nob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nob ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SPIKE_ADE12 SPIKE_ADE12] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CXCAR to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface (By similarity). | |||
== 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/no/1nob_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=1nob ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Binding of virus particles to specific host cell surface receptors is known to be an obligatory step in infection even though the molecular basis for these interactions is not well characterized. The crystal structure of the adenovirus fiber knob domain in complex with domain I of its human cellular receptor, coxsackie and adenovirus receptor (CAR), is presented here. Surface-exposed loops on knob contact one face of CAR, forming a high-affinity complex. Topology mismatches between interacting surfaces create interfacial solvent-filled cavities and channels that may be targets for antiviral drug therapy. The structure identifies key determinants of binding specificity, which may suggest ways to modify the tropism of adenovirus-based gene therapy vectors. | |||
Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR.,Bewley MC, Springer K, Zhang YB, Freimuth P, Flanagan JM Science. 1999 Nov 19;286(5444):1579-83. PMID:10567268<ref>PMID:10567268</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Human adenovirus | <div class="pdbe-citations 1nob" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Bewley | <references/> | ||
[[Category: Flanagan | __TOC__ | ||
[[Category: Freimuth | </StructureSection> | ||
[[Category: Springer | [[Category: Human adenovirus 12]] | ||
[[Category: Zhang | [[Category: Large Structures]] | ||
[[Category: Bewley MC]] | |||
[[Category: Flanagan JM]] | |||
[[Category: Freimuth P]] | |||
[[Category: Springer K]] | |||
[[Category: Zhang YB]] | |||
Latest revision as of 12:23, 16 August 2023
KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12
Structural highlights
FunctionSPIKE_ADE12 Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CXCAR to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBinding of virus particles to specific host cell surface receptors is known to be an obligatory step in infection even though the molecular basis for these interactions is not well characterized. The crystal structure of the adenovirus fiber knob domain in complex with domain I of its human cellular receptor, coxsackie and adenovirus receptor (CAR), is presented here. Surface-exposed loops on knob contact one face of CAR, forming a high-affinity complex. Topology mismatches between interacting surfaces create interfacial solvent-filled cavities and channels that may be targets for antiviral drug therapy. The structure identifies key determinants of binding specificity, which may suggest ways to modify the tropism of adenovirus-based gene therapy vectors. Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR.,Bewley MC, Springer K, Zhang YB, Freimuth P, Flanagan JM Science. 1999 Nov 19;286(5444):1579-83. PMID:10567268[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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