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DOI no:
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Proc Natl Acad Sci U S A
90:6320-6324
(1993)
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PubMed id:
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Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA.
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A.Jacobo-Molina,
J.Ding,
R.G.Nanni,
A.D.Clark,
X.Lu,
C.Tantillo,
R.L.Williams,
G.Kamer,
A.L.Ferris,
P.Clark.
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ABSTRACT
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The crystal structure of a ternary complex of human immunodeficiency virus type
1 reverse transcriptase (HIV-1 RT) heterodimer (p66/p51), a 19-base/18-base
double-stranded DNA template-primer, and a monoclonal antibody Fab fragment has
been determined at 3.0 A resolution. The four individual subdomains of RT that
make up the polymerase domains of p66 and p51 are named fingers, palm, thumb,
and connection [Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A. &
Steitz, T. A. (1992) Science 256, 1783-1790]. The overall folding of the
subdomains is similar in p66 and p51 but the spatial arrangements of the
subdomains are dramatically different. The template-primer has A-form and B-form
regions separated by a significant bend (40-45 degrees). The most numerous
nucleic acid interactions with protein occur primarily along the sugar-phosphate
backbone of the DNA and involve amino acid residues of the palm, thumb, and
fingers of p66. Highly conserved regions are located in the p66 palm near the
polymerase active site. These structural elements, together with two
alpha-helices of the thumb of p66, act as a clamp to position the
template-primer relative to the polymerase active site. The 3'-hydroxyl of the
primer terminus is close to the catalytically essential Asp-110, Asp-185, and
Asp-186 residues at the active site and is in a position for nucleophilic attack
on the alpha-phosphate of an incoming nucleoside triphosphate. The structure of
the HIV-1 RT/DNA/Fab complex should aid our understanding of general mechanisms
of nucleic acid polymerization. AIDS therapies may be enhanced by a fuller
understanding of drug inhibition and resistance emerging from these studies.
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PubMed id
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S.Tuske,
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J.Jäger,
J.Wang,
L.A.Kohlstaedt,
A.J.Chirino,
J.M.Friedman,
P.A.Rice,
and
T.A.Steitz
(1994).
Structure of the binding site for nonnucleoside inhibitors of the reverse transcriptase of human immunodeficiency virus type 1.
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Proc Natl Acad Sci U S A,
91,
3911-3915.
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PDB code:
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S.Loya,
M.Bakhanashvili,
R.Tal,
S.H.Hughes,
P.L.Boyer,
and
A.Hizi
(1994).
Enzymatic properties of two mutants of reverse transcriptase of human immunodeficiency virus type 1 (tyrosine 181-->isoleucine and tyrosine 188-->leucine), resistant to nonnucleoside inhibitors.
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AIDS Res Hum Retroviruses,
10,
939-946.
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T.Hermann,
T.Meier,
M.Götte,
and
H.Heumann
(1994).
The 'helix clamp' in HIV-1 reverse transcriptase: a new nucleic acid binding motif common in nucleic acid polymerases.
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| |
Nucleic Acids Res,
22,
4625-4633.
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T.Rubinek,
S.Loya,
M.Shaharabany,
S.H.Hughes,
P.K.Clark,
and
A.Hizi
(1994).
The catalytic properties of the reverse transcriptase of the lentivirus equine infectious anemia virus.
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| |
Eur J Biochem,
219,
977-983.
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T.Unge,
S.Knight,
R.Bhikhabhai,
S.Lövgren,
Z.Dauter,
K.Wilson,
and
B.Strandberg
(1994).
2.2 A resolution structure of the amino-terminal half of HIV-1 reverse transcriptase (fingers and palm subdomains).
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Structure,
2,
953-961.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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only a partial list as not all journals are covered by
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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