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• W2617316683 abstract "The human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins (Env) mediate viral entry and are the sole target of neutralizing antibodies. Recent studies show that the metastable HIV-1 Env trimer can transit among three conformational states: State 1, State 3, and State 2, corresponding to the closed, open and intermediate conformations, respectively. During virus entry, binding to the CD4 receptor drives Env from state 1 to state 3. In the unliganded Env, transitions from the closed (State 1) conformation are restrained by intramolecular interactions among different Env residues, which regulate HIV-1 Env conformation. Releasing the specific restraints on State 1 Env leads to increased occupancy of State 2, which is a functional conformation on the entry pathway and an obligate intermediate between State 1 and State 3. Frequent sampling of intermediate State 2 allows HIV-1 to infect cells expressing low levels of CD4, and leads to resistance to several broadly neutralizing antibodies as well as small-molecule inhibitors. Recent findings provide new mechanistic insights into the function and inhibition of HIV-1 Env and will contribute to the development of new therapeutic and prophylactic interventions to combat HIV-1." @default.
• W2617316683 created "2017-06-05" @default.
• W2617316683 creator A5066679273 @default.
• W2617316683 creator A5071476197 @default.
• W2617316683 date "2017-05-10" @default.
• W2617316683 modified "2023-10-16" @default.
• W2617316683 title "An Entry-Competent Intermediate State of the HIV-1 Envelope Glycoproteins" @default.
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• W2617316683 doi "https://doi.org/10.14800/rci.1544" @default.
• W2617316683 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5526225" @default.
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