title: Structural similarity between the p17 matrix protein of HIV-1 and interferon-gamma.
abstract: The human immunodeficiency virus (HIV) matrix protein, p17, forms the outer shell of the core of the virus, lining the inner surface of the viral membrane. The protein has several key functions. It orchestrates viral assembly via targeting signals that direct the gag precursor polyprotein, p55, to the host cell membrane and it interacts with the transmembrane protein, gp41, to retain the env-encoded proteins in the virus. In addition, p17 contains a nuclear localization signal that directs the preintegration complex to the nucleus of infected cells. This permits the virus to infect productively non-dividing cells, a distinguishing feature of HIV and other lentiviruses. We have determined the solution structure of p17 by nuclear magnetic resonance (NMR) with a root-mean square deviation for the backbone of the well-defined regions of 0.9 A. It consists of four helices connected by short loops and an irregular, mixed beta-sheet which provides a positively charged surface for interaction with the inner layer of the membrane. The helical topology is unusual; the Brookhaven protein database contains only one similar structure, that of the immune modulator interferon-gamma.
authors.affiliation: Department of Biochemistry, University of Oxford, UK.
authors.forename: S
authors.initials: S
authors.lastname: Matthews
authors.forename: P
authors.initials: P
authors.lastname: Barlow
authors.forename: J
authors.initials: J
authors.lastname: Boyd
authors.forename: G
authors.initials: G
authors.lastname: Barton
authors.forename: R
authors.initials: R
authors.lastname: Russell
authors.forename: H
authors.initials: H
authors.lastname: Mills
authors.forename: M
authors.initials: M
authors.lastname: Cunningham
authors.forename: N
authors.initials: N
authors.lastname: Meyers
authors.forename: N
authors.initials: N
authors.lastname: Burns
authors.forename: N
authors.initials: N
authors.lastname: Clark
mesh_terms: D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D003196:Computer Graphics; D016208:Databases, Factual; D004926:Escherichia coli; D015683:Gene Products, gag / Q000737:chemistry*; D015488:HIV Antigens / Q000737:chemistry*; D015497:HIV-1; D006801:Humans; D007371:Interferon-gamma / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins; D054301:gag Gene Products, Human Immunodeficiency Virus
chemical_list: D015683:Gene Products, gag; D015488:HIV Antigens; D011994:Recombinant Proteins; D014764:Viral Proteins; D054301:gag Gene Products, Human Immunodeficiency Virus; C054858:p17 protein, Human Immunodeficiency Virus Type 1; D007371:Interferon-gamma