Capturing conformational transitions of full-length PDK1 that dictate kinase substrate selectivity

Laura Martínez-Arenas; Jose R. Bayascas

doi:10.1126/scisignal.adh5114

Capturing conformational transitions of full-length PDK1 that dictate kinase substrate selectivity

Laura Martínez-Arenas, Jose R. Bayascas

Departament de Bioquímica i de Biologia Molecular

Producció científica: Contribució a revista › Article › Recerca › Avaluat per experts

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PDK1 is a constitutively active master kinase that can phosphorylate and activate as many as 24 enzymes, all belonging to the AGC family of serine-threonine protein kinases. In this issue of Science Signaling, Sacerdoti et al. uncover how allosteric communication between different functional domains directs the selectivity of PDK1 toward particular subsets of substrates.

Idioma original	Anglès
Número d’article	eadh5114
Pàgines (de-a)	eadh5114
Revista	Science Signaling
Volum	16
Número	789
DOIs	https://doi.org/10.1126/scisignal.adh5114
Estat de la publicació	Publicada - 13 de juny 2023

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10.1126/scisignal.adh5114

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abstract = "PDK1 is a constitutively active master kinase that can phosphorylate and activate as many as 24 enzymes, all belonging to the AGC family of serine-threonine protein kinases. In this issue of Science Signaling, Sacerdoti et al. uncover how allosteric communication between different functional domains directs the selectivity of PDK1 toward particular subsets of substrates.",

author = "Laura Mart{\'i}nez-Arenas and Bayascas, \{Jose R.\}",

note = "Publisher Copyright: Copyright {\textcopyright} 2023 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.",

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Capturing conformational transitions of full-length PDK1 that dictate kinase substrate selectivity

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