5aga

Crystal structure of the Helicase domain of human DNA polymerase theta in complex with AMPPNP

spinqualitylabelsall models 5aga, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5aga is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: ANP, FLC, K, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed DNA polymerase theta (Poltheta) has been identified as a crucial alternative non-homologous end-joining factor in mammalian cells. Poltheta 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 Poltheta 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. Poltheta exists as a tetramer both in the crystals and in solution. We propose a model for DNA binding to the Poltheta helicase domain in the context of the Poltheta tetramer, which suggests a role for the helicase domain in strand annealing of DNA templates for subsequent processing by the polymerase domain. Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway.,Newman JA, Cooper CD, Aitkenhead H, Gileadi O Structure. 2015 Dec 1;23(12):2319-30. doi: 10.1016/j.str.2015.10.014. PMID:26636256 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DNA polymerase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA