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Dataset

X-ray Diffraction Images of SNX17 PX domain

The University of Queensland
Brett Collins (Aggregated by)
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ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=http://dimer.uq.edu.au/projects/snx17px/experiments/px12/datasets/px12.html&rft.title=X-ray Diffraction Images of SNX17 PX domain&rft.identifier=http://dimer.uq.edu.au/projects/snx17px/experiments/px12/datasets/px12.html&rft.publisher=The University of Queensland&rft.description=This dataset contains diffraction images of the SNX17 PX domain. Two distinct phox-homology (PX)-domain-containing proteins, sorting nexin (SNX) 17 and SNX27, are critical regulators of recycling from endosomes to the cell surface. In this study we demonstrate that SNX17, SNX27, and SNX31 all possess a novel 4.1/ezrin/radixin/moesin (FERM)-like domain. Studies of the SNX17 PX domain coupled with cellular localization experiments reveal the mechanistic basis for endosomal localization of the PX-FERM-like proteins, and structures of SNX17 and SNX27 determined by small angle X-ray scattering show that they adopt non-self-assembling, modular structures in solution.&rft.creator=Brett Collins&rft.date=2013&rft.relation=http://www.pdb.org/pdb/explore/explore.do?structureId=3LUI&rft.relation=http://www.ncbi.nlm.nih.gov/pubmed/21512128&rft_rights=Diffraction Image Experiment Repository http://creativecommons.org/licenses/by/3.0/rdf&rft_rights=This data is jointly owned by the University of Queensland and current and/or former students of the University of Queensland&rft_subject=Crystallography&rft_subject=X-ray Diffraction&rft_subject=Structural Biology (incl. Macromolecular Modelling)&rft_subject=Biochemistry and Cell Biology&rft_subject=Biological Sciences&rft_subject=Expanding Knowledge in the Chemical Sciences&rft_subject=Expanding Knowledge&rft_subject=Expanding Knowledge&rft_subject=Expanding Knowledge in the Medical and Health Sciences&rft_subject=Expanding Knowledge in the Biological Sciences&rft.type=dataset&rft.language=English Go to Data Provider

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Diffraction Image Experiment Repository
http://creativecommons.org/licenses/by/3.0/rdf

This data is jointly owned by the University of Queensland and current and/or former students of the University of Queensland

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This data is freely available via the DIMER website

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This dataset contains diffraction images of the SNX17 PX domain. Two distinct phox-homology (PX)-domain-containing proteins, sorting nexin (SNX) 17 and SNX27, are critical regulators of recycling from endosomes to the cell surface. In this study we demonstrate that SNX17, SNX27, and SNX31 all possess a novel 4.1/ezrin/radixin/moesin (FERM)-like domain. Studies of the SNX17 PX domain coupled with cellular localization experiments reveal the mechanistic basis for endosomal localization of the PX-FERM-like proteins, and structures of SNX17 and SNX27 determined by small angle X-ray scattering show that they adopt non-self-assembling, modular structures in solution.