
Understanding the structure of the native HIV-1 envelope spike protein is critical for the development of vaccines and antiviral therapies. In this issue of Structure, Guttman and colleagues use hydrogen-deuterium exchange (HDX) to provide new insights into the structure of the HIV-1 Env trimer and enhance our understanding of how HIV-1 Env is activated for virus fusion.
Structural Biology, CD4 Antigens, env Gene Products, Human Immunodeficiency Virus, Humans, Protein Multimerization, Protein Structure, Quaternary, Molecular Biology
Structural Biology, CD4 Antigens, env Gene Products, Human Immunodeficiency Virus, Humans, Protein Multimerization, Protein Structure, Quaternary, Molecular Biology
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