Cryo-EM structure of a CD4-bound open HIV-1 envelope trimer reveals structural rearrangements of the gp120 V1V2 loop
Copyright policy )Cryo-EM structure of a CD4-bound open HIV-1 envelope trimer reveals structural rearrangements of the gp120 V1V2 loop
Significance The HIV-1 envelope (Env) glycoprotein exists in multiple conformations on virion surfaces. Although the closed Env state is well characterized, less is known about open Env conformations stabilized by host receptor (CD4) binding. We solved an 8.9-Å structure of a partially open CD4-bound Env trimer by single particle cryo-EM. In the CD4-bound Env, the gp120 V1V2 loops were displaced by ∼40 Å from their positions at the trimer apex. The displaced V1V2 loops were at the sides of the open trimer in positions adjacent to, and interacting with, the three bound CD4s. These results are relevant to understanding CD4-induced conformational changes leading to coreceptor binding and fusion, and HIV-1 Env conformational dynamics, and describe a target structure relevant to drug design and vaccine efforts.
- University of California, San Francisco United States
- Howard Hughes Medical Institute United States
- California Institute of Technology United States
Models, Molecular, Protein Conformation, 610, HIV Envelope Protein gp120, HIV-1 Env trimer, conformational change, Models, Humans, Prevention, Cryoelectron Microscopy, Molecular, HIV-1 coreceptor, CD4, HIV Envelope Protein gp41, Infectious Diseases, Good Health and Well Being, HEK293 Cells, CD4 Antigens, HIV/AIDS, cryo-EM, Protein Multimerization, Infection, Protein Binding
Models, Molecular, Protein Conformation, 610, HIV Envelope Protein gp120, HIV-1 Env trimer, conformational change, Models, Humans, Prevention, Cryoelectron Microscopy, Molecular, HIV-1 coreceptor, CD4, HIV Envelope Protein gp41, Infectious Diseases, Good Health and Well Being, HEK293 Cells, CD4 Antigens, HIV/AIDS, cryo-EM, Protein Multimerization, Infection, Protein Binding
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