2iny: Difference between revisions
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<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 [ | <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'>[ | <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 == | ||
[[ | [[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]] | ||
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</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/> | ||
