title: Structure of an HIV-2 gp120 in Complex with CD4.
abstract: HIV-2 is a nonpandemic form of the virus causing AIDS, and the majority of HIV-2-infected patients exhibit long-term nonprogression. The HIV-1 and HIV-2 envelope glycoproteins, the sole targets of neutralizing antibodies, share 30 to 40% identity. As a first step in understanding the reduced pathogenicity of HIV-2, we solved a 3.0-Å structure of an HIV-2 gp120 bound to the host receptor CD4, which reveals structural similarity to HIV-1 gp120 despite divergence in amino acid sequence.
authors.affiliation: Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, California, USA.
authors.forename: Yunji W
authors.initials: YW
authors.lastname: Davenport
authors.affiliation: Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, California, USA.
authors.forename: Anthony P
authors.initials: AP
authors.lastname: West
authors.affiliation: Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, California, USA bjorkman@caltech.edu.
authors.forename: Pamela J
authors.initials: PJ
authors.lastname: Bjorkman
mesh_terms: D015704:CD4 Antigens / Q000737:chemistry*; D018360:Crystallography, X-Ray; D015699:HIV Envelope Protein gp120 / Q000737:chemistry*; D015498:HIV-2 / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120