Document 0175
 DOCN  M9480175
 TI    Three-dimensional 1H NMR structure of the nucleocapsid protein NCp10 of
       Moloney murine leukemia virus.
 DT    9410
 AU    Demene H; Jullian N; Morellet N; de Rocquigny H; Cornille F; Maigret B;
       Roques BP; Departemente de Pharmacochimie Moleculaire et Structurale,
       U266; INSERM-URA D 1500 CNRS, Faculte de Pharmacie, Paris, France.
 SO    J Biomol NMR. 1994 Mar;4(2):153-70. Unique Identifier : AIDSLINE
       MED/94289983
 AB    The nucleocapsid protein of Moloney murine leukemia virus (NCp10) is a
       56-amino acid protein which contains one zinc finger of the
       CysX2CysX4HisX4Cys form, a highly conserved motif present in most
       retroviruses and retroelements. At pH > or = 5, NCp10 binds one zinc
       atom and the complexation induces a folding of the CysX2CysX4HEsX4Cys
       box, similar to that observed for the zinc-binding domains of HIV-1 NC
       protein. The three-dimensional structure of NCp10 has been determined in
       aqueous solution by 600 MHz 1H NMR spectroscopy. The proton resonances
       could be almost completely assigned by means of phase-sensitive
       double-quantum-filtered COSY, TOCSY and NOESY techniques. NOESY spectra
       yielded 597 relevant structural constraints, which were used as input
       for distance geometry calculations with DIANA. Further refinement was
       performed by minimization with the program AMBER, which was modified by
       introducing a zinc force field. The solution structure is characterized
       by a well-defined central zinc finger (rmsd of 0.747 +/- 0.209 A for
       backbone atoms and 1.709 +/- 0.187 A when all atoms are considered),
       surrounded by flexible N- and C-terminal domains. The Tyr28, Trp35,
       Lys37, Lys41 and Lys42 residues, which are essential for activity, lie
       on the same face of the zinc finger, forming a bulge structure probably
       involved in viral RNA binding. The significance of these structural
       characteristics for the various biological functions of the protein is
       discussed, taking into account the results obtained with various
       mutants.
 DE    Amino Acid Sequence  Conserved Sequence  Gene Products,
       gag/*CHEMISTRY/CHEMICAL SYNTHESIS  Hydrogen  Mathematics  Models,
       Molecular  Molecular Sequence Data  Moloney Leukemia Virus/*CHEMISTRY
       Nuclear Magnetic Resonance/METHODS  *Protein Conformation  Support,
       Non-U.S. Gov't  Viral Core Proteins/*CHEMISTRY/CHEMICAL SYNTHESIS  Zinc
       Fingers  JOURNAL ARTICLE

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