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| | <StructureSection load='1p69' size='340' side='right'caption='[[1p69]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='1p69' size='340' side='right'caption='[[1p69]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1p69]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade12 Ade12] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P69 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P69 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1p69]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [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=1P69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P69 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kac|1kac]], [[1p6a|1p6a]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28282 ADE12]), CXADR, CAR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p69 OCA], [https://pdbe.org/1p69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p69 RCSB], [https://www.ebi.ac.uk/pdbsum/1p69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p69 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p69 OCA], [http://pdbe.org/1p69 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p69 RCSB], [http://www.ebi.ac.uk/pdbsum/1p69 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p69 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). [[http://www.uniprot.org/uniprot/CXAR_HUMAN CXAR_HUMAN]] Component of the epithelial apical junction complex that is essential for the tight junction integrity. Proposed to function as a homophilic cell adhesion molecule. Recruits MPDZ to intercellular contact sites. Probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN) through adhesive interactions with AMICA1/JAML located in the plasma membrane of PMN.<ref>PMID:9096397</ref> <ref>PMID:11734628</ref> <ref>PMID:12297051</ref> <ref>PMID:15800062</ref> | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p6/1p69_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p6/1p69_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ade12]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Human adenovirus 12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bewley, M C]] | + | [[Category: Bewley MC]] |
| - | [[Category: Flanagan, J M]] | + | [[Category: Flanagan JM]] |
| - | [[Category: Freimuth, P]] | + | [[Category: Freimuth P]] |
| - | [[Category: Graziano, V]] | + | [[Category: Graziano V]] |
| - | [[Category: Howitt, J]] | + | [[Category: Howitt J]] |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Viral protein-receptor complex]]
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| - | [[Category: Virus]]
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| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The majority of adenovirus serotypes can bind to the coxsackievirus and adenovirus receptor (CAR) on human cells despite only limited conservation of the amino acid residues that comprise the receptor-binding sites of these viruses. Using a fluorescence anisotropy-based assay, we determined that the recombinant knob domain of the fiber protein from adenovirus serotype (Ad) 2 binds the soluble, N-terminal domain (domain 1 (D1)) of CAR with 8-fold greater affinity than does the recombinant knob domain from Ad12. Homology modeling predicted that the increased affinity of Ad2 knob for CAR D1 could result from additional contacts within the binding interface contributed by two residues, Ser408 and Tyr477, which are not conserved in the Ad12 knob. Consistent with this structural model, substitution of serine and tyrosine for the corresponding residues in the Ad12 knob (P417S and S489Y) increased the binding affinity by 4- and 8-fold, respectively, whereas the double mutation increased binding affinity 10-fold. X-ray structure analysis of Ad12 knob mutants P417S and S489Y indicated that both substituted residues potentially could form additional hydrogen bonds across the knob-CAR interface. Structural changes resulting from these mutations were highly localized, implying that the high tolerance for surface variation conferred by the stable knob scaffold can minimize the impact of antigenic drift on binding specificity and affinity during evolution of virus serotypes. Our results suggest that the interaction of knob domains from different adenovirus serotypes with CAR D1 can be accurately modeled using the Ad12 knob-CAR D1 crystal structure as a template.
Structural basis for variation in adenovirus affinity for the cellular coxsackievirus and adenovirus receptor.,Howitt J, Bewley MC, Graziano V, Flanagan JM, Freimuth P J Biol Chem. 2003 Jul 11;278(28):26208-15. Epub 2003 Apr 25. PMID:12716886[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Howitt J, Bewley MC, Graziano V, Flanagan JM, Freimuth P. Structural basis for variation in adenovirus affinity for the cellular coxsackievirus and adenovirus receptor. J Biol Chem. 2003 Jul 11;278(28):26208-15. Epub 2003 Apr 25. PMID:12716886 doi:http://dx.doi.org/10.1074/jbc.M301492200
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