3zif: Difference between revisions
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</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=3zif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zif OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zif RCSB], [http://www.ebi.ac.uk/pdbsum/3zif PDBsum]</span></td></tr> | </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=3zif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zif OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zif RCSB], [http://www.ebi.ac.uk/pdbsum/3zif PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CAPSH_ADEB3 CAPSH_ADEB3]] 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). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
