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

Departamento de Bioquímica y Biología Molecular

Producción científica: Contribución a una revista › Artículo › Investigación › revisión exhaustiva

Resumen

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	Inglés
Número de artículo	eadh5114
Páginas (desde-hasta)	eadh5114
Publicación	Science Signaling
Volumen	16
N.º	789
DOI	https://doi.org/10.1126/scisignal.adh5114
Estado	Publicada - 13 jun 2023

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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.}",

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

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