Name: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate. So far, in addition to halogen atoms, other non-metallic atoms can become part of the aromatic heterocycle, and the target ring system is still aromatic. Compound: Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, is researched, Molecular C18H20N2O12, CAS is 70539-42-3, about Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41.
Envelope oligomerization is thought to serve crucial functions during the life cycle of human immunodeficiency virus type 1 (HIV-1). We recently reported that virus entry requires coiled-coil formation of the leucine zipper-like domain of the HIV-1 transmembrane envelope glycoprotein gp41. To determine the oligomeric state mediated by this region of the envelope, we have expressed the zipper motif as a fusion partner with the monomeric maltose-binding protein of Escherichia coli. The biophys. properties of this protein were characterized by velocity and equilibrium sedimentation, size exclusion chromatog., light scattering, and chem. crosslinking analyses. Results indicate that the leucine zipper sequence from HIV-1 is capable of multimerizing much larger and otherwise monomeric proteins into extremely stable tetramers. Recombinant proteins containing an alanine or a serine substitution at a critical isoleucine residue within the zipper region were also generated and similarly analyzed. The alanine- and serine-substituted proteins behaved as tetrameric and monomeric species, resp., consistent with the influence of these same substitutions on the helical coiled-coil structure of synthetic peptide models. On the basis of these findings, we propose that the fusogenic gp41 structure involves tetramerization of the leucine zipper domain which is situated ∼30 residues from the N-terminal fusion peptide sequence.
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Reference:
Benzofuran – Wikipedia,
Benzofuran | C8H6O – PubChem