title: The HIV-1 Env trimer in HD.
abstract: 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.
authors.affiliation: Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536, USA.
authors.forename: James B
authors.initials: JB
authors.lastname: Munro
authors.affiliation: Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536, USA. Electronic address: walther.mothes@yale.edu.
authors.forename: Walther
authors.initials: W
authors.lastname: Mothes
mesh_terms: D015704:CD4 Antigens / Q000737:chemistry*; D006801:Humans; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D054299:env Gene Products, Human Immunodeficiency Virus / Q000737:chemistry*
chemical_list: D015704:CD4 Antigens; D054299:env Gene Products, Human Immunodeficiency Virus