3tg7: Difference between revisions

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==Crystal structure of Adenovirus serotype 5 hexon at 1.6A resolution==

== Structural highlights ==

<table><tr><td colspan='2'>[[3tg7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Human_adenovirus_5 Human adenovirus 5~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TG7 FirstGlance]. <br>

<table><tr><td colspan='2'>[[3tg7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade05 Ade05]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TG7 FirstGlance]. <br>

</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=3tg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tg7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3tg7 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=3tg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tg7 OCA], [http://pdbe.org/3tg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3tg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tg7 ProSAT]</span></td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/~~HEX_ADE05 HEX_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.

[[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.

__TOC__

</StructureSection>

[[Category: ~~Human adenovirus 5~~]]

[[Category: Ade05]]

[[Category: Baker, A H]]

[[Category: Isaacs, N W]]

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 ==Crystal structure of Adenovirus serotype 5 hexon at 1.6A resolution==
 <StructureSection load='3tg7' size='340' side='right' caption='[[3tg7]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3tg7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_5 Human adenovirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TG7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3tg7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade05 Ade05]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TG7 FirstGlance]. <br>
-</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=3tg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tg7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3tg7 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=3tg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tg7 OCA], [http://pdbe.org/3tg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3tg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tg7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEX_ADE05 HEX_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.
+[[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.
 __TOC__
 </StructureSection>
-[[Category: Human adenovirus 5]]
+[[Category: Ade05]]
 [[Category: Baker, A H]]
 [[Category: Isaacs, N W]]