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Title
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Buried surface analysis of HIV-1 reverse transcriptase p66/p51 heterodimer and its interaction with dsDNA template/primer.
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Authors
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J.Ding,
A.Jacobo-Molina,
C.Tantillo,
X.Lu,
R.G.Nanni,
E.Arnold.
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Ref.
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J Mol Recognit, 1994,
7,
157-161.
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PubMed id
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Abstract
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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.
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