1z66
From Proteopedia
(Difference between revisions)
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<StructureSection load='1z66' size='340' side='right'caption='[[1z66]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1z66' size='340' side='right'caption='[[1z66]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1z66]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1z66]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Flavivirus_langat Flavivirus langat]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1Z66 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yzo|1yzo]], [[1svb|1svb]], [[1pjw|1pjw]], [[1s6n|1s6n]]</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=1z66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z66 OCA], [https://pdbe.org/1z66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z66 RCSB], [https://www.ebi.ac.uk/pdbsum/1z66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z66 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://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]] | ||
Revision as of 08:17, 10 November 2021
NMR solution structure of domain III of E-protein of tick-borne Langat flavivirus (no RDC restraints)
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