title: Structure of the transmembrane domain of HIV-1 envelope glycoprotein.
abstract: HIV-1 envelope spike (Env) is a heavily glycosylated, type I membrane protein that mediates fusion of viral and cell membranes to initiate infection. It is also a primary target of neutralizing antibodies and thus an important candidate for vaccine development. We have recently reported a nuclear magnetic resonance structure of the transmembrane (TM) domain of HIV-1 Env reconstituted in a membrane-like environment. Taking HIV-1 as an example, we discuss here how a TM domain can anchor, stabilize, and modulate a viral envelope spike and how its high-resolution structure can contribute to understanding viral membrane fusion and to immunogen design.
authors.affiliation: Division of Molecular Medicine, Department of Pediatrics, Boston Children's Hospital, Harvard Medical School, Boston, MA, USA.
authors.forename: Bing
authors.initials: B
authors.lastname: Chen
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
authors.forename: James J
authors.initials: JJ
authors.lastname: Chou
mesh_terms: D000595:Amino Acid Sequence; D019302:HIV Envelope Protein gp160 / Q000737:chemistry* / Q000276:immunology / Q000502:physiology; D015497:HIV-1 / Q000737:chemistry* / Q000502:physiology; D008561:Membrane Fusion / Q000502:physiology; D008958:Models, Molecular; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D014614:Vaccines, Synthetic / Q000737:chemistry
chemical_list: D019302:HIV Envelope Protein gp160; D014614:Vaccines, Synthetic
keywords: HIV; envelope; nuclear magnetic resonance; transmembrane