1z66

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1z66]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z66 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1z66]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z66 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yzo|1yzo]], [[1svb|1svb]], [[1pjw|1pjw]], [[1s6n|1s6n]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yzo|1yzo]], [[1svb|1svb]], [[1pjw|1pjw]], [[1s6n|1s6n]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z66 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z66 RCSB], [http://www.ebi.ac.uk/pdbsum/1z66 PDBsum]</span></td></tr>
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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=1z66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z66 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z66 RCSB], [http://www.ebi.ac.uk/pdbsum/1z66 PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/POLG_LANVY POLG_LANVY]] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). 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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Langat virus]]
[[Category: Langat virus]]
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[[Category: Cowburn, D.]]
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[[Category: Cowburn, D]]
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[[Category: Dutta, K.]]
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[[Category: Dutta, K]]
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[[Category: Fox, R O.]]
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[[Category: Fox, R O]]
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[[Category: Mukherjee, M.]]
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[[Category: Mukherjee, M]]
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[[Category: White, M A.]]
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[[Category: White, M A]]
[[Category: Viral protein]]
[[Category: Viral protein]]

Revision as of 23:47, 24 December 2014

NMR solution structure of domain III of E-protein of tick-borne Langat flavivirus (no RDC restraints)

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