ArticleStructure (London, England : 1993)2008
Cryo-EM structure of the DNA-dependent protein kinase catalytic subunit at subnanometer resolution reveals alpha helices and insight into DNA binding.
Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Structural studies of protein-nucleic acid complexes: A brief overview of the selected techniques.Computational and structural biotechnology journal · 2023Review
- Structural analysis of the basal state of the Artemis:DNA-PKcs complex.Nucleic acids research · 2022Article
- Role of PRKDC in cancer initiation, progression, and treatment.Cancer cell international · 2021Review
- X-ray scattering reveals disordered linkers and dynamic interfaces in complexes and mechanisms for DNA double-strand break repair impacting cell and cancer biology.Protein science : a publication of the Protein Society · 2021Review
- Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM.Progress in biophysics and molecular biology · 2021Article
- The Multifaceted Roles of Ku70/80.International journal of molecular sciences · 2021Review
- Structure of an activated DNA-PK and its implications for NHEJ.Molecular cell · 2021Article
- Structural step forward for NHEJ.Cell research · 2017Article
- A Process of Resection-Dependent Nonhomologous End Joining Involving the Goddess Artemis.Trends in biochemical sciences · 2017Review
- DNA requirements for interaction of the C-terminal region of Ku80 with the DNA-dependent protein kinase catalytic subunit (DNA-PKcs).DNA repair · 2017Article
- Insights into Rad3 kinase recruitment from the crystal structure of the DNA damage checkpoint protein Rad26.The Journal of biological chemistry · 2017Article
- DNA Double-Strand Break Resection Occurs during Non-homologous End Joining in G1 but Is Distinct from Resection during Homologous Recombination.Molecular cell · 2017Article
- DNA-PKcs, Allostery, and DNA Double-Strand Break Repair: Defining the Structure and Setting the Stage.Methods in enzymology · 2017Article
- What Combined Measurements From Structures and Imaging Tell Us About DNA Damage Responses.Methods in enzymology · 2017Review
- Lysines 3241 and 3260 of DNA-PKcs are important for genomic stability and radioresistance.Biochemical and biophysical research communications · 2016Article
- ATR-mediated regulation of nuclear and cellular plasticity.DNA repair · 2016Review
- The Dimeric Architecture of Checkpoint Kinases Mec1ATR and Tel1ATM Reveal a Common Structural Organization.The Journal of biological chemistry · 2016Article
- A network of SMG-8, SMG-9 and SMG-1 C-terminal insertion domain regulates UPF1 substrate recruitment and phosphorylation.Nucleic acids research · 2015Article
- The DNA-dependent protein kinase: A multifunctional protein kinase with roles in DNA double strand break repair and mitosis.Progress in biophysics and molecular biology · 2015Review
- Recognition of DNA Termini by the C-Terminal Region of the Ku80 and the DNA-Dependent Protein Kinase Catalytic Subunit.PloS one · 2015Article
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Abstract
The DNA-dependent protein kinase catalytic subunit (DNA-PKcs) regulates the nonhomologous end joining pathway for repair of double-stranded DNA (dsDNA) breaks. Here, we present a 7A resolution structure of DNA-PKcs determined by cryo-electron microscopy single-particle reconstruction. This structure is composed of density rods throughout the molecule that are indicative of alpha helices and reveals structural features not observed in lower resolution EM structures. Docking of homology models into the DNA-PKcs structure demonstrates that up to eight helical HEAT repeat motifs fit well within the density. Surprisingly, models for the kinase domain can be docked into either the crown or base of the molecule at this resolution, although real space refinement suggests that the base location is the best fit. We propose a model for the interaction of DNA with DNA-PKcs in which one turn of dsDNA enters the central channel and interacts with a resolved alpha-helical protrusion.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.