Document 1025
 DOCN  M9541025
 TI    Buried surface analysis of HIV-1 reverse transcriptase p66/p51
       heterodimer and its interaction with dsDNA template/primer.
 DT    9504
 AU    Ding J; Jacobo-Molina A; Tantillo C; Lu X; Nanni RG; Arnold E; Center
       for Advanced Biotechnology and Medicine (CABM), Rutgers; University,
       Piscataway, NJ 08854-5638.
 SO    J Mol Recognit. 1994 Jun;7(2):157-61. Unique Identifier : AIDSLINE
       MED/95127266
 AB    The p66/p51 human immunodeficiency virus type 1 reverse transcriptase is
       a heterodimer with identical N-terminal amino acid sequences. The enzyme
       contains two polymerization domains and one RNase H domain, which is
       located at the C-terminus of the p66 subunit. Both polymerization
       domains fold into four individual subdomains that are not arranged in a
       similar fashion, forming an unusually asymmetric dimer. The complexity
       of the RT p66/p51 heterodimer structure is simplified using
       solvent-accessibility surface areas to describe the buried surface area
       of contact among the different subdomains. In addition, the RT/DNA
       contacts in the recently published RT/DNA/Fab structure [Jacobo-Molina
       et al., Proc. Natl Acad. Sci. USA, 90, 6320-6324 (1993)] are described
       using the same approach. Finally, the RT/DNA complex is compared with
       other dimeric DNA-binding proteins. It was found that the size of the
       protein and the extent of the dimer interface were not directly related
       to the extent of contact between the protein and the DNA. Furthermore,
       RT, the only protein that is not a sequence-specific DNA binding protein
       in this analysis, had the largest surface of interaction with the
       nucleic acid.
 DE    Binding Sites  DNA/*METABOLISM  DNA Primers  Human  HIV-1/*ENZYMOLOGY
       In Vitro  Macromolecular Systems  Models, Molecular  Molecular Structure
       Molecular Weight  Protein Conformation  Reverse
       Transcriptase/*CHEMISTRY/*METABOLISM  Substrate Specificity  Support,
       Non-U.S. Gov't  Support, U.S. Gov't, P.H.S.  JOURNAL ARTICLE  REVIEW
       REVIEW, TUTORIAL

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