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.
Guardado en:
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: | |
Acceso en línea: | https://doaj.org/article/96b3e407ffe647c5b54ac432fe843d79 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Chimeric design of pyrrolysyl-tRNA synthetase/tRNA pairs and canonical synthetase/tRNA pairs for genetic code expansion
por: Wenlong Ding, et al.
Publicado: (2020) -
Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organisms
por: Spencer O. Moen, et al.
Publicado: (2017) -
Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics
por: Takaaki Akaike, et al.
Publicado: (2017) -
A threonyl-tRNA synthetase-mediated translation initiation machinery
por: Seung Jae Jeong, et al.
Publicado: (2019) -
Transforming a pair of orthogonal tRNA-aminoacyl-tRNA synthetase from Archaea to function in mammalian cells.
por: Gabrielle Nina Thibodeaux, et al.
Publicado: (2010)