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| | <StructureSection load='1p30' size='340' side='right'caption='[[1p30]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1p30' size='340' side='right'caption='[[1p30]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1p30]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade05 Ade05]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1rux 1rux]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P30 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1p30]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_adenovirus_5 Human adenovirus 5]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1rux 1rux]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P30 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rux|1rux]], [[1p2z|1p2z]], [[1dhx|1dhx]]</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]] 2.5Å</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=1p30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p30 OCA], [http://pdbe.org/1p30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p30 RCSB], [http://www.ebi.ac.uk/pdbsum/1p30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p30 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=1p30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p30 OCA], [https://pdbe.org/1p30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p30 RCSB], [https://www.ebi.ac.uk/pdbsum/1p30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p30 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAPSH_ADE05 CAPSH_ADE05]] Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein (By similarity). Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus. | + | [https://www.uniprot.org/uniprot/CAPSH_ADE05 CAPSH_ADE05] Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein (By similarity). Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1p30" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1p30" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ade05]] | + | [[Category: Human adenovirus 5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Burnett, R M]] | + | [[Category: Burnett RM]] |
| - | [[Category: Kuser, P R]] | + | [[Category: Kuser PR]] |
| - | [[Category: Rux, J J]] | + | [[Category: Rux JJ]] |
| - | [[Category: Adenovirus]]
| + | |
| - | [[Category: Coat protein]]
| + | |
| - | [[Category: Hexon]]
| + | |
| - | [[Category: Jellyroll]]
| + | |
| - | [[Category: Type 5]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Virus]]
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| Structural highlights
Function
CAPSH_ADE05 Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein (By similarity). Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus.
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
A major impediment to the use of adenovirus as a gene therapy vector and for vaccine applications is the host immune response to adenovirus hexon-the major protein component of the icosahedral capsid. A solution may lie in novel vectors with modified or chimeric hexons designed to evade the immune response. To facilitate this approach, we have distinguished the portion of hexon that all serotypes have in common from the hypervariable regions that are responsible for capsid diversity and type-specific immunogenicity. The common hexon core-conserved because it forms the viral capsid-sets boundaries to the regions where modifications can be made to produce nonnative hexons. The core has been defined from the large and diverse set of known hexon sequences by an accurate alignment based on the newly refined crystal structures of human adenovirus types 2 (Ad2) and Ad5 hexon. Comparison of the two hexon models, which are the most accurate so far, reveals that over 90% of the residues in each have three-dimensional positions that closely match. Structures for more distant hexons were predicted by building molecular models of human Ad4, chimpanzee adenovirus (AdC68), and fowl adenovirus 1 (FAV1 or CELO). The five structures were then used to guide the alignment of the 40 full-length (>900 residues) hexon sequences in public databases. Distance- and parsimony-based phylogenetic trees are consistent and reveal evolutionary relationships between adenovirus types that parallel those of their animal hosts. The combination of crystallography, molecular modeling, and phylogenetic analysis defines a conserved molecular core that can serve as the armature for the directed design of novel hexons.
Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution x-ray crystallographic, molecular modeling, and sequence-based methods.,Rux JJ, Kuser PR, Burnett RM J Virol. 2003 Sep;77(17):9553-66. PMID:12915569[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rux JJ, Kuser PR, Burnett RM. Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution x-ray crystallographic, molecular modeling, and sequence-based methods. J Virol. 2003 Sep;77(17):9553-66. PMID:12915569
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