Document 0570
 DOCN  M9490570
 TI    Structural similarity between the p17 matrix protein of HIV-1 and
       interferon-gamma.
 DT    9411
 AU    Matthews S; Barlow P; Boyd J; Barton G; Russell R; Mills H; Cunningham
       M; Meyers N; Burns N; Clark N; et al; Department of Biochemistry,
       University of Oxford, UK.
 SO    Nature. 1994 Aug 25;370(6491):666-8. Unique Identifier : AIDSLINE
       MED/94344244
 AB    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.
 DE    Amino Acid Sequence  Cloning, Molecular  Computer Graphics  Databases,
       Factual  Escherichia coli  Gene Products, gag/*CHEMISTRY  Human  HIV
       Antigens/*CHEMISTRY  *HIV-1  Interferon Type II/*CHEMISTRY  Molecular
       Sequence Data  Nuclear Magnetic Resonance  Protein Conformation
       Recombinant Proteins  Sequence Homology, Amino Acid  Support, Non-U.S.
       Gov't  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).