View source for 1emz


==SOLUTION STRUCTURE OF FRAGMENT (350-370) OF THE TRANSMEMBRANE DOMAIN OF HEPATITIS C ENVELOPE GLYCOPROTEIN E1==
<StructureSection load='1emz' size='340' side='right'caption='[[1emz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1emz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepacivirus_C Hepacivirus C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EMZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1emz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1emz OCA], [https://pdbe.org/1emz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1emz RCSB], [https://www.ebi.ac.uk/pdbsum/1emz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1emz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9Q3N3_9HEPC Q9Q3N3_9HEPC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Oligomerization of viral envelope proteins is essential to control virus assembly and fusion. The transmembrane domains (TMDs) of hepatitis C virus envelope glycoproteins E1 and E2 have been shown to play multiple functions during the biogenesis of E1E2 heterodimer. This makes them very unique among known transmembrane sequences. In this report, we used alanine scanning insertion mutagenesis in the TMDs of E1 and E2 to examine their role in the assembly of E1E2 heterodimer. Alanine insertion within the center of the TMDs of E1 or E2 or in the N-terminal part of the TMD of E1 dramatically reduced heterodimerization, demonstrating the essential role played by these domains in the assembly of hepatitis C virus envelope glycoproteins. To better understand the alanine scanning data obtained for the TMD of E1 which contains GXXXG motifs, we analyzed by circular dichroism and nuclear magnetic resonance the three-dimensional structure of the E1-(350-370) peptide encompassing the N-terminal sequence of the TMD of E1 involved in heterodimerization. Alanine scanning results and the three-dimensional molecular model we obtained provide the first framework for a molecular level understanding of the mechanism of hepatitis C virus envelope glycoprotein heterodimerization.

The transmembrane domains of hepatitis C virus envelope glycoproteins E1 and E2 play a major role in heterodimerization.,Op De Beeck A, Montserret R, Duvet S, Cocquerel L, Cacan R, Barberot B, Le Maire M, Penin F, Dubuisson J J Biol Chem. 2000 Oct 6;275(40):31428-37. PMID:10807921<ref>PMID:10807921</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1emz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hepacivirus C]]
[[Category: Large Structures]]
[[Category: Barberot B]]
[[Category: Cacan R]]
[[Category: Cocquerel L]]
[[Category: Dubuisson J]]
[[Category: Duvet S]]
[[Category: Le Maire M]]
[[Category: Montserret R]]
[[Category: Op De Beeck A]]
[[Category: Penin F]]