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PDBsum entry 5a9f
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References listed in PDB file
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Key reference
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Title
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Structure of the helicase domain of DNA polymerase theta reveals a possible role in the microhomology-Mediated end-Joining pathway.
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Authors
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J.A.Newman,
C.D.Cooper,
H.Aitkenhead,
O.Gileadi.
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Ref.
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Structure, 2015,
23,
2319-2330.
[DOI no: ]
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PubMed id
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Abstract
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DNA polymerase theta (Polθ) has been identified as a crucial alternative
non-homologous end-joining factor in mammalian cells. Polθ is upregulated in a
range of cancer cell types defective in homologous recombination, and knockdown
has been shown to inhibit cell survival in a subset of these, making it an
attractive target for cancer treatment. We present crystal structures of the
helicase domain of human Polθ in the presence and absence of bound nucleotides,
and a characterization of its DNA-binding and DNA-stimulated ATPase activities.
Comparisons with related helicases from the Hel308 family identify several
unique features. Polθ exists as a tetramer both in the crystals and in
solution. We propose a model for DNA binding to the Polθ helicase domain in the
context of the Polθ tetramer, which suggests a role for the helicase domain in
strand annealing of DNA templates for subsequent processing by the polymerase
domain.
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