       Document 0055
 DOCN  M9590055
 TI    [Conformation of crystalline 3'-nitro-2',3'-dideoxythymidine and
       properties of its 5'-triphosphate as a terminator substrate of
       retroviral reverse transcriptase]
 DT    9509
 AU    Kuznetsova EV; Kukhanova MK; Gurskaia GV; Fedorov II; Ias'ko MV;
       Chattopadiiyaya J; Kraevskii AA; University of Uppsala, Sweden.
 SO    Mol Biol (Mosk). 1995 Mar-Apr;29(2):407-14. Unique Identifier : AIDSLINE
       MED/95303107
 AB    The structure of new nucleoside--3'-nitro-2',3'-dideoxythymidine (NIT)
       possessing moderate anti HIV activity in MT-4 cell culture was
       investigated by X-ray analysis. These data showed that conformation of
       NIT in crystal is similar to that of one of crystallographically
       independent forms of 3'-azido-2',3'-dideoxythymidine.
       3'-Nitro-2',3'-dideoxythymidine 5'-triphosphate (NITTP) was synthesized
       and its ability to inhibit human and viral DNA polymerases was studied.
       NITTP proved to be effective and highly selective terminating substrate
       of DNA synthesis catalyzed by HIV and AMV reverse transcriptases. Human
       DNA polymerase alpha as well as DNA polymerase beta (rat liver),
       terminal deoxynucleotidyltransferase (calf thymus) or HSV-1 and CMV DNA
       polymerases did not incorporate NITTP into a growing DNA chain.
 DE    Animal  Base Sequence  Cattle  Crystallography, X-Ray  DNA
       Polymerases/ANTAGONISTS & INHIB  DNA Primers  English Abstract  Human
       HIV-1/*ENZYMOLOGY  Molecular Conformation  Molecular Sequence Data
       Myeloblastosis Virus, Avian/ENZYMOLOGY  Rats  Reverse
       Transcriptase/ANTAGONISTS & INHIB/*METABOLISM  Substrate Specificity
       Thymine Nucleotides/*CHEMISTRY  JOURNAL ARTICLE

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

