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| | <StructureSection load='2j12' size='340' side='right'caption='[[2j12]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='2j12' size='340' side='right'caption='[[2j12]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2j12]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Adenovirus_type_37 Adenovirus type 37] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J12 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2j12]] 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_D37 Human adenovirus D37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J12 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1uxa|1uxa]], [[1uxb|1uxb]], [[1uxe|1uxe]], [[1eaj|1eaj]], [[1f5w|1f5w]], [[1jew|1jew]], [[1kac|1kac]], [[1p69|1p69]], [[1p6a|1p6a]], [[1rsf|1rsf]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=2j12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j12 OCA], [https://pdbe.org/2j12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j12 RCSB], [https://www.ebi.ac.uk/pdbsum/2j12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j12 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=2j12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j12 OCA], [https://pdbe.org/2j12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j12 RCSB], [https://www.ebi.ac.uk/pdbsum/2j12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j12 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q80S15_9ADEN Q80S15_9ADEN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Adenovirus type 37]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Human adenovirus D37]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Billet, O]] | + | [[Category: Billet O]] |
| - | [[Category: Cusack, S]] | + | [[Category: Cusack S]] |
| - | [[Category: Kremer, E J]] | + | [[Category: Kremer EJ]] |
| - | [[Category: Lortat-Jacob, H]] | + | [[Category: Lortat-Jacob H]] |
| - | [[Category: Seiradake, E]] | + | [[Category: Seiradake E]] |
| - | [[Category: Ad37]]
| + | |
| - | [[Category: Adenovirus]]
| + | |
| - | [[Category: Car]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Coxsackievirus]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Had37]]
| + | |
| - | [[Category: Host-virus interaction]]
| + | |
| - | [[Category: Immunoglobulin domain]]
| + | |
| - | [[Category: Lipoprotein]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Palmitate]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Tight junction]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Viral protein-receptor complex]]
| + | |
| Structural highlights
Function
Q80S15_9ADEN
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
Adenovirus fibers from most serotypes bind the D1 domain of coxsackie and adenovirus receptor (CAR), although the binding residues are not strictly conserved. To understand this further, we determined the crystal structures of canine adenovirus serotype 2 (CAV-2) and the human adenovirus serotype 37 (HAd37) in complex with human CAR D1 at 2.3 and 1.5A resolution, respectively. Structure comparison with the HAd12 fiber head-CAR D1 complex showed that the overall topology of the interaction is conserved but that the interfaces differ in number and identity of interacting residues, shape complementarity, and degree of conformational adaptation. Using surface plasmon resonance, we characterized the binding affinity to CAR D1 of wild type and mutant CAV-2 and HAd37 fiber heads. We found that CAV-2 has the highest affinity but fewest direct interactions, with the reverse being true for HAd37. Moreover, we found that conserved interactions can have a minor contribution, whereas serotype-specific interactions can be essential. These results are discussed in the light of virus evolution and design of adenovirus vectors for gene transfer.
Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor.,Seiradake E, Lortat-Jacob H, Billet O, Kremer EJ, Cusack S J Biol Chem. 2006 Nov 3;281(44):33704-16. Epub 2006 Aug 21. PMID:16923808[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Seiradake E, Lortat-Jacob H, Billet O, Kremer EJ, Cusack S. Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor. J Biol Chem. 2006 Nov 3;281(44):33704-16. Epub 2006 Aug 21. PMID:16923808 doi:http://dx.doi.org/10.1074/jbc.M605316200
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