Conformational states dynamically populated by a kinase determine its function

Protein kinases intrinsically sample a number of conformational states with distinct catalytic and binding activities. We used nuclear magnetic resonance spectroscopy to describe in atomic-level detail how Abl kinase interconverts between an active and two discrete inactive structures. Extensive dif...

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Vydáno v:	Science (American Association for the Advancement of Science) Ročník 370; číslo 6513
Hlavní autoři:	Xie, Tao, Saleh, Tamjeed, Rossi, Paolo, Kalodimos, Charalampos G
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 09.10.2020
Témata:	Biocatalysis Genes, abl Humans Imatinib Mesylate - chemistry Mutation Nuclear Magnetic Resonance, Biomolecular Oligopeptides - chemistry Oligopeptides - genetics Protein Domains Protein Kinase Inhibitors - chemistry Protein Structure, Secondary Protein-Tyrosine Kinases - chemistry Protein-Tyrosine Kinases - genetics
ISSN:	1095-9203, 1095-9203
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