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M94A2063.TXT
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1994-10-24
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Document 2063
DOCN M94A2063
TI RNase H domain of HIV-2: crystal structure and reconstitution of the
activity.
DT 9412
AU Hostomska Z; Matthews DA; Knighton DR; Hostomsky Z
SO Int Conf AIDS. 1994 Aug 7-12;10(1):39 (abstract no. 128A). Unique
Identifier : AIDSLINE ICA10/94370512
AB The HIV reverse transcriptase (RT) is a multifunctional enzyme which
displays DNA- and RNA-dependent DNA polymerase and RNase H activities.
RNase H activity, which resides in 15 kD C-terminal region of p66
subunit of RT, is required for viral replication. To design compounds
active against RNase H of both HIV-1 and HIV-2 it is important to
understand the molecular details of their structures. We characterized
enzymatic activity of HIV-2 RNase H and compared crystal structures of
HIV-1 and HIV-2 RNase H. HIV-2 RNase H domain (of ISY strain) is 60%
identical to that of HIV-1 (strain BH10). They are no insertion or
deletions. We found that while the RNase H domain exhibit no detectable
activity when expressed separately, the activity can be reconstituted by
combining RNase H and DNA polymerase domains. Interestingly, the
activity of isolated HIV-2 RNase H can be reconstituted not only in the
presence of the HIV-2 polymerase domain but also with the HIV-1
polymerase domain. It suggests that sites involved in specific
interdomain interactions in RT are conserved between HIV-1 and HIV-2.
The purified HIV-2 RNase H domain was crystallized in a triclinic cell
and its structure was determined. The structural model of HIV-2 RNase H
will be presented.
DE DNA Polymerases/CHEMISTRY HIV-1/ENZYMOLOGY HIV-2/*ENZYMOLOGY
Molecular Structure Ribonuclease H, Calf Thymus/*CHEMISTRY/GENETICS
MEETING ABSTRACT
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).