Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines

Bicyclic azetidine inhibitors are promising antimalarials that target the Plasmodium cytosolic phenylalanine tRNAsynthetase (cFRS). Here, Sharma et al. provide the biochemical and structural basis of its mechanism using co-crystal structure of PvcFRS with BRD1389.

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Autores principales:	Manmohan Sharma, Nipun Malhotra, Manickam Yogavel, Karl Harlos, Bruno Melillo, Eamon Comer, Arthur Gonse, Suhel Parvez, Branko Mitasev, Francis G. Fang, Stuart L. Schreiber, Amit Sharma
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/96b3e407ffe647c5b54ac432fe843d79
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spelling	oai:doaj.org-article:96b3e407ffe647c5b54ac432fe843d792021-12-02T14:01:26ZStructural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines10.1038/s41467-020-20478-52041-1723https://doaj.org/article/96b3e407ffe647c5b54ac432fe843d792021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20478-5https://doaj.org/toc/2041-1723Bicyclic azetidine inhibitors are promising antimalarials that target the Plasmodium cytosolic phenylalanine tRNAsynthetase (cFRS). Here, Sharma et al. provide the biochemical and structural basis of its mechanism using co-crystal structure of PvcFRS with BRD1389.Manmohan SharmaNipun MalhotraManickam YogavelKarl HarlosBruno MelilloEamon ComerArthur GonseSuhel ParvezBranko MitasevFrancis G. FangStuart L. SchreiberAmit SharmaNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Manmohan Sharma Nipun Malhotra Manickam Yogavel Karl Harlos Bruno Melillo Eamon Comer Arthur Gonse Suhel Parvez Branko Mitasev Francis G. Fang Stuart L. Schreiber Amit Sharma Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines
description	Bicyclic azetidine inhibitors are promising antimalarials that target the Plasmodium cytosolic phenylalanine tRNAsynthetase (cFRS). Here, Sharma et al. provide the biochemical and structural basis of its mechanism using co-crystal structure of PvcFRS with BRD1389.
format	article
author	Manmohan Sharma Nipun Malhotra Manickam Yogavel Karl Harlos Bruno Melillo Eamon Comer Arthur Gonse Suhel Parvez Branko Mitasev Francis G. Fang Stuart L. Schreiber Amit Sharma
author_facet	Manmohan Sharma Nipun Malhotra Manickam Yogavel Karl Harlos Bruno Melillo Eamon Comer Arthur Gonse Suhel Parvez Branko Mitasev Francis G. Fang Stuart L. Schreiber Amit Sharma
author_sort	Manmohan Sharma
title	Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines
title_short	Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines
title_full	Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines
title_fullStr	Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines
title_full_unstemmed	Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines
title_sort	structural basis of malaria parasite phenylalanine trna-synthetase inhibition by bicyclic azetidines
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/96b3e407ffe647c5b54ac432fe843d79
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Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines

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