1z3r: Difference between revisions
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<StructureSection load='1z3r' size='340' side='right'caption='[[1z3r]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | <StructureSection load='1z3r' size='340' side='right'caption='[[1z3r]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1z3r]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1z3r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ohfv Ohfv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z3R FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z3r OCA], [https://pdbe.org/1z3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z3r RCSB], [https://www.ebi.ac.uk/pdbsum/1z3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z3r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/Q80J38_9FLAV Q80J38_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] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 19:36, 3 November 2021
Solution structure of the Omsk Hemhorraghic Fever Envelope Protein Domain IIISolution structure of the Omsk Hemhorraghic Fever Envelope Protein Domain III
Structural highlights
Function[Q80J38_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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have solved the NMR solution structure of domain III from the Omsk hemorrhagic fever virus envelope protein and report the first sequencing of the Guriev strain of this virus. Important structural differences between tick-borne flaviviruses, such as OHFV and TBE, and mosquito-borne flaviviruses, such as West Nile virus, are discussed. Structure of the envelope protein domain III of Omsk hemorrhagic fever virus.,Volk DE, Chavez L, Beasley DW, Barrett AD, Holbrook MR, Gorenstein DG Virology. 2006 Jul 20;351(1):188-95. Epub 2006 May 2. PMID:16647096[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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