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Letter
Nature Structural Biology  5, 276 - 279 (1998)
doi:10.1038/nsb0498-276

Capture of an early fusion-active conformation of HIV-1 gp41

Rika A. Furuta1, Carl T. Wild2, Yongkai Weng1 & Carol D. Weiss1, 3

  1Office of Vaccines, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration (FDA), Bldg. 29, Room 532, HFM-413, 29 Lincoln Dr., Bethesda, Maryland 20892-4555, USA.

  2Biotech Research Laboratories, 217 Perry Parkway, Gaithersburg, Maryland 20877, USA.

  3email: cdweiss@helix.nih.gov

Using an inhibitory synthetic peptide (DP-178) from HIV-1 gp41, we have trapped HIV-1 envelope glycoprotein (Env) undergoing conformational changes during virus entry. Our data show that DP-178 binds gp41 and inhibits Env-mediated membrane fusion after gp120 interacts with cellular receptors, indicating that conformational changes involving the coiled coil domain of gp41 are required for entry. Capture of this fusion-active conformation of Env provides insights into the early events leading to Env-mediated membrane fusion.


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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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