ArticleActa crystallographica. Section D, Biological crystallography2012
S-SAD phasing study of death receptor 6 and its solution conformation revealed by SAXS.
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- The Intricate Role of Caspase-6 and Death Receptor-6 in Neurodegenerative Diseases.Cell biochemistry and biophysics · 2026Review
- A Structural and Functional Perspective of Death Receptor 6.Frontiers in pharmacology · 2022Review
- Article
- Crystal structure of murine 4-1BB and its interaction with 4-1BBL support a role for galectin-9 in 4-1BB signaling.The Journal of biological chemistry · 2018Article
- Contemporary Use of Anomalous Diffraction in Biomolecular Structure Analysis.Methods in molecular biology (Clifton, N.J.) · 2017Review
- aKMT Catalyzes Extensive Protein Lysine Methylation in the Hyperthermophilic Archaeon Sulfolobus islandicus but is Dispensable for the Growth of the Organism.Molecular & cellular proteomics : MCP · 2016Article
- Data collection with a tailored X-ray beam size at 2.69 Å wavelength (4.6 keV): sulfur SAD phasing of Cdc23(Nterm).Acta crystallographica. Section D, Structural biology · 2016Article
- In-vacuum long-wavelength macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2016Article
- Combination Therapy of LysGH15 and Apigenin as a New Strategy for Treating Pneumonia Caused by Staphylococcus aureus.Applied and environmental microbiology · 2016Article
- Principles of antibody-mediated TNF receptor activation.Cell death and differentiation · 2015Review
- Native SAD is maturing.IUCrJ · 2015Review
- The crystal structure of DR6 in complex with the amyloid precursor protein provides insight into death receptor activation.Genes & development · 2015Article
- Structural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin.PLoS pathogens · 2014Article
- Structural analysis of asparaginyl endopeptidase reveals the activation mechanism and a reversible intermediate maturation stage.Cell research · 2014Article
- Structure of the Leanyer orthobunyavirus nucleoprotein-RNA complex reveals unique architecture for RNA encapsidation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Localization and orientation of heavy-atom cluster compounds in protein crystals using molecular replacement.Acta crystallographica. Section D, Biological crystallography · 2013Article
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Authors and funding
11 authors.
Funding
Abstract
A subset of tumour necrosis factor receptor (TNFR) superfamily members contain death domains in their cytoplasmic tails. Death receptor 6 (DR6) is one such member and can trigger apoptosis upon the binding of a ligand by its cysteine-rich domains (CRDs). The crystal structure of the ectodomain (amino acids 1-348) of human death receptor 6 (DR6) encompassing the CRD region was phased using the anomalous signal from S atoms. In order to explore the feasibility of S-SAD phasing at longer wavelengths (beyond 2.5 Å), a comparative study was performed on data collected at wavelengths of 2.0 and 2.7 Å. In spite of sub-optimal experimental conditions, the 2.7 Å wavelength used for data collection showed potential for S-SAD phasing. The results showed that the R(ano)/R(p.i.m.) ratio is a good indicator for monitoring the anomalous data quality when the anomalous signal is relatively strong, while d''/sig(d'') calculated by SHELXC is a more sensitive and stable indicator applicable for grading a wider range of anomalous data qualities. The use of the `parameter-space screening method' for S-SAD phasing resulted in solutions for data sets that failed during manual attempts. SAXS measurements on the ectodomain suggested that a dimer defines the minimal physical unit of an unliganded DR6 molecule in solution.
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