ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase
ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase
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Publisher
London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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Scope and Contents
Contents
The crystal structure of prolyl tRNA synthetase simultaneously bound to its substrate ATP and its inhibitor halofuginone, a derivative of a compound used to treat malaria, indicates that (through interactions with ATP) halofuginone occupies both the amino acid and tRNA binding sites on the synthetase, revealing a new model for developing synthetase...
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Full title
ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3569068
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3569068
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ISSN
0028-0836
E-ISSN
1476-4687
DOI
10.1038/nature11774
