1emz
From Proteopedia
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SOLUTION STRUCTURE OF FRAGMENT (350-370) OF THE TRANSMEMBRANE DOMAIN OF HEPATITIS C ENVELOPE GLYCOPROTEIN E1
Overview
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.
About this Structure
1EMZ is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
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