|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Adenovirus Ad3 fibre head== | | ==Adenovirus Ad3 fibre head== |
| - | <StructureSection load='1h7z' size='340' side='right' caption='[[1h7z]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='1h7z' size='340' side='right'caption='[[1h7z]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h7z]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade03 Ade03]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H7Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1h7z]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_adenovirus_B3 Human adenovirus B3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H7Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1knb|1knb]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7z OCA], [http://pdbe.org/1h7z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h7z RCSB], [http://www.ebi.ac.uk/pdbsum/1h7z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h7z ProSAT]</span></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=1h7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7z OCA], [https://pdbe.org/1h7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h7z RCSB], [https://www.ebi.ac.uk/pdbsum/1h7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h7z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SPIKE_ADE03 SPIKE_ADE03]] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Heparan sulfate might also play a role in virus binding. | + | [https://www.uniprot.org/uniprot/SPIKE_ADE03 SPIKE_ADE03] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Heparan sulfate might also play a role in virus binding. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 33: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ade03]] | + | [[Category: Human adenovirus B3]] |
| - | [[Category: Burmeister, W P]] | + | [[Category: Large Structures]] |
| - | [[Category: Cusack, S]] | + | [[Category: Burmeister WP]] |
| - | [[Category: Drouet, E]] | + | [[Category: Cusack S]] |
| - | [[Category: Durmort, C]] | + | [[Category: Drouet E]] |
| - | [[Category: Mitraki, A]] | + | [[Category: Durmort C]] |
| - | [[Category: Schoehn, G]] | + | [[Category: Mitraki A]] |
| - | [[Category: Stehlin, C]] | + | [[Category: Schoehn G]] |
| - | [[Category: Ad3]]
| + | [[Category: Stehlin C]] |
| - | [[Category: Adenovirus]]
| + | |
| - | [[Category: Cell receptor recognition]]
| + | |
| - | [[Category: Fibre]]
| + | |
| - | [[Category: Receptor]]
| + | |
| Structural highlights
Function
SPIKE_ADE03 Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Heparan sulfate might also play a role in virus binding.
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
Adenoviruses of serotype Ad3 (subgenus B) use a still-unknown host cell receptor for viral attachment, whereas viruses from all other known subgenera use the coxsackie and adenovirus receptor (CAR). The receptor binding domain (head) of the Ad3 fiber protein has been expressed in Escherichia coli inclusion bodies. After denaturation and renaturation using a rapid dilution method, crystals of trimeric head were obtained. The 1.6 A resolution X-ray structure shows a strict conservation of the beta-sheet scaffold of the protein very similar to the head structures of the CAR-binding serotypes Ad2, Ad5, and Ad12. The conformation of the loops is different, with the exception of the AB loop, which forms the center of the interface in the Ad12-CAR complex structure. The structure explains why a mutation in Ad5 of one residue in the AB loop to glutamic acid, as in Ad3, abrogates binding to CAR. It is possible that the Ad3 receptor binding site is nevertheless situated similar to the CAR binding site, although it cannot be excluded that other regions of the relatively hydrophobic head surface may be used.
Structure of the fiber head of Ad3, a non-CAR-binding serotype of adenovirus.,Durmort C, Stehlin C, Schoehn G, Mitraki A, Drouet E, Cusack S, Burmeister WP Virology. 2001 Jul 5;285(2):302-12. PMID:11437664[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Durmort C, Stehlin C, Schoehn G, Mitraki A, Drouet E, Cusack S, Burmeister WP. Structure of the fiber head of Ad3, a non-CAR-binding serotype of adenovirus. Virology. 2001 Jul 5;285(2):302-12. PMID:11437664 doi:10.1006/viro.2001.0967
|
