       Document 0581
 DOCN  M9610581
 TI    The DNA-binding domain of HIV-1 integrase has an SH3-like fold.
 DT    9601
 AU    Eijkelenboom AP; Lutzke RA; Boelens R; Plasterk RH; Kaptein R; Hard K;
       Bijvoet Center for Biomolecular Research, Utrecht University, The;
       Netherlands.
 SO    Nat Struct Biol. 1995 Sep;2(9):807-10. Unique Identifier : AIDSLINE
       MED/96018619
 AB    We have determined the solution structure of the DNA-binding domain of
       HIV-1 integrase by nuclear magnetic resonance spectroscopy. In solution,
       this carboxyterminal region of integrase forms a homodimer, consisting
       of two structures that closely resemble Src-homology 3 (SH3) domains.
       Lys 264, previously identified by mutagenesis studies to be important
       for DNA binding of the integrase, as well as several adjacent basic
       amino acids are solvent exposed. The identification of an SH3-like
       domain in integrase provides a new potential target for drug design.
 DE    src Homology Domains  Amino Acid Sequence  Binding Sites
       Chromatography, Gel  DNA/*METABOLISM  DNA
       Nucleotidyltransferases/*CHEMISTRY/GENETICS/*METABOLISM
       HIV-1/ENZYMOLOGY  Molecular Sequence Data  Mutation  Nuclear Magnetic
       Resonance  Protein Conformation  Protein Folding  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).

