3irc

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<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=3irc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3irc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3irc RCSB], [http://www.ebi.ac.uk/pdbsum/3irc PDBsum], [http://www.topsan.org/Proteins/CSGID/3irc TOPSAN]</span></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=3irc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3irc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3irc RCSB], [http://www.ebi.ac.uk/pdbsum/3irc PDBsum], [http://www.topsan.org/Proteins/CSGID/3irc TOPSAN]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/Q9J7C6_9FLAV Q9J7C6_9FLAV]] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS026470_004_099774]
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</StructureSection>
</StructureSection>

Revision as of 20:37, 25 December 2014

Crystal structure analysis of dengue-1 envelope protein domain III

3irc, resolution 2.25Å

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