Conformation of trimeric envelope glycoproteins: the CD4-dependent membrane fusion mechanism of HIV-1.

摘要: The HIV-1 envelope glycoproteins are assembled by the trimeric gp120s and gp41s proteins. gp120 binds sequentially to CD4 coreceptor for initiating virus entry. Because of noncovalent interaction heavy glycosylation glycoproteins, it is highly difficult determine entire structure now. Such question extremely limits our good understanding membrane fusion mechanism. Here, a novel reasonable assembly model was proposed based on conformational dynamics gp120-gp41 complex gp41, respectively. As heptad repeat sequences in gp41 C-terminal enormous flexibility. On contrary, N-terminal likely present stable three-helical bundle due strong nonpolar interaction, they were predicted associate three alpha1 helixes from non-neutralizing face inner domain, which quite similar core structure. leads formation complex. In complex, not only perfectly complementary symmetrical distribution around but also different flexibility degree structural domains. Thus, new can well explain numerous experimental phenomena, plenty information, elucidate effectively mechanism, direct further develop vaccine inhibitors.