Document 0707
 DOCN  M9590707
 TI    Three Dimensional Structure of the Core Domain of HIV-1 Integrase
 DT    9509
 AU    Dyda F; Hickman AB; Jenkins TM; Engelman A; Craigie A; Davies DR;
       Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD
 SO    NIH Conf Retroviral Integrase. 1995 Jan 19-20;:(Session III, speakers'
       abstracts - unpaged). Unique Identifier : AIDSLINE AIDS/95920012
 AB    The crystal structure of the core domain of HIV-1 integrase (residues 50
       to 212), which is fully active for disintegration, will be described at
       2.5  resolution. The structure reveals topological similarity to other
       polynucleotidyl transferases like (RNase H), Mu Transposase and the
       Holliday junction resolvase RuvC. There are significant differences,
       however, in the relative positions of some of the helices with respect
       to the central five- stranded beta sheet common in all of the above
       enzymes. The active site is identified by the position of two of the
       three conserved and catalytically essential carboxylate residues. Based
       on charge distribution, regions with likely involvement with the DNA
       substrate are located. The core domain forms a dimer in the crystal
       structure with a large solvent inaccessible interface of 1300 2 per
       monomer. This dimer is stabilized by several hydrogen bond interactions
       across the interface. The mutated residue (185 Lys) which was
       responsible for the soluble and crystallizable protein is located at the
       rim of this interface interacting with both the solvent and with the
       other monomer. This dimer assembly places the two active sites 35 apart,
       which implies that the active oligomeric form of HIV-1 integrase is at
       least a tetramer.
 DE    Binding Sites  Crystallography, X-Ray  DNA
       Nucleotidyltransferases/*CHEMISTRY/METABOLISM  HIV-1/*ENZYMOLOGY
       Hydrogen Bonding  *Protein Conformation  MEETING ABSTRACT

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