|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2iny' size='340' side='right'caption='[[2iny]], [[Resolution|resolution]] 3.90Å' scene=''> | | <StructureSection load='2iny' size='340' side='right'caption='[[2iny]], [[Resolution|resolution]] 3.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2iny]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Fowl_adenovirus_1 Fowl adenovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2INY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2INY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2iny]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fowl_adenovirus_1 Fowl adenovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2INY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2INY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p30|1p30]], [[1p2z|1p2z]], [[1hx6|1hx6]], [[1m3y|1m3y]], [[2bbd|2bbd]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p30|1p30]], [[1p2z|1p2z]], [[1hx6|1hx6]], [[1m3y|1m3y]], [[2bbd|2bbd]]</div></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=2iny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iny OCA], [http://pdbe.org/2iny PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iny RCSB], [http://www.ebi.ac.uk/pdbsum/2iny PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iny 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=2iny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iny OCA], [https://pdbe.org/2iny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iny RCSB], [https://www.ebi.ac.uk/pdbsum/2iny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iny ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAPSH_ADEG1 CAPSH_ADEG1]] 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. 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 (By similarity). | + | [[https://www.uniprot.org/uniprot/CAPSH_ADEG1 CAPSH_ADEG1]] 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. 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 (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 28: |
Line 28: |
| | </div> | | </div> |
| | <div class="pdbe-citations 2iny" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2iny" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[CAPSH_ADEG1] 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. 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 (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
CELO (chicken embryo lethal orphan) virus is an avian adenovirus that is being developed as a gene transfer vector. Its trimeric major coat protein (942 residues, 106,709 Da) has 42% sequence identity to human adenovirus type 2 (AdH2) hexon and 45% to AdH5 hexon. For structural studies, the growth of CELO virus has been optimized, and its hexon purified and crystallized. The hexon crystals, the first non-human example, diffract to 3.9 A resolution. Molecular replacement using the AdH5 model was used to identify the location of the CELO hexon within the unit cell. There is one hexon monomer in the asymmetric unit of the trigonal space group P321 (a=b=157.8 A, c=114.2 A, gamma=120 degrees) and the solvent content is 67.8%. The hexons pack in a hexagonal honeycomb so that large approximately 100 A diameter channels run through the entire crystal. This remarkable property of the crystals lends itself to their exploitation as a nanomaterial. Structural studies on CELO will elucidate the differences between avian and human adenoviruses and contribute to a better understanding of adenoviruses with non-human hosts.
Nanoporous crystals of chicken embryo lethal orphan (CELO) adenovirus major coat protein, hexon.,Xu L, Benson SD, Burnett RM J Struct Biol. 2007 Feb;157(2):424-31. Epub 2006 Sep 14. PMID:17071105[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Xu L, Benson SD, Burnett RM. Nanoporous crystals of chicken embryo lethal orphan (CELO) adenovirus major coat protein, hexon. J Struct Biol. 2007 Feb;157(2):424-31. Epub 2006 Sep 14. PMID:17071105 doi:http://dx.doi.org/10.1016/j.jsb.2006.08.017
|
