Core Structure of gp41 from the HIV Envelope Glycoprotein

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Core Structure of gp41 from the HIV Envelope Glycoprotein

The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) consists of a complex of gp120 and gp41. gp120 determines viral tropism by binding to target-cell receptors, while gp41 mediates fusion between viral and cellular membranes. Previous studies identified an alpha-helical domain within gp41 composed of a trimer of two interacting peptides. The crystal structure of this comple...

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Structure of the Core of the HIV-1 gp120 Exterior Envelope Glycoprotein

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Structure of the transmembrane domain of HIV-1 envelope glycoprotein.

HIV-1 envelope spike (Env) is a heavily glycosylated, type I membrane protein that mediates fusion of viral and cell membranes to initiate infection. It is also a primary target of neutralizing antibodies and thus an important candidate for vaccine development. We have recently reported a nuclear magnetic resonance structure of the transmembrane (TM) domain of HIV-1 Env reconstituted in a membr...

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Small molecules that bind the inner core of gp41 and inhibit HIV envelope-mediated fusion.

HIV-1 enters cells by membrane fusion, mediated by the trimeric viral envelope glycoprotein gp160, which is processed by a single proteolytic cleavage into stably associated gp120 and gp41. The gp120/gp41 trimer can be triggered to undergo an irreversible conformational change. Using a protein-based assay designed to mimic the gp41 conformational change, we screened for small molecules that pre...

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ژورنال

عنوان ژورنال: Cell

سال: 1997

ISSN: 0092-8674

DOI: 10.1016/s0092-8674(00)80205-6