Capturing conformational transitions of full-length PDK1 that dictate kinase substrate selectivity
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 , Sacerdoti . uncover how allosteric communication between different functional domains directs the selectivi...
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| Veröffentlicht in: | Science signaling 2023-06, Vol.16 (789), p.eadh5114-eadh5114 |
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| container_end_page | eadh5114 |
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| container_issue | 789 |
| container_start_page | eadh5114 |
| container_title | Science signaling |
| container_volume | 16 |
| creator | Martínez-Arenas, Laura Bayascas, Jose R |
| description | 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
, Sacerdoti
. uncover how allosteric communication between different functional domains directs the selectivity of PDK1 toward particular subsets of substrates. |
| doi_str_mv | 10.1126/scisignal.adh5114 |
| format | Article |
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| fulltext | fulltext |
| identifier | ISSN: 1945-0877 |
| ispartof | Science signaling, 2023-06, Vol.16 (789), p.eadh5114-eadh5114 |
| issn | 1945-0877 1937-9145 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2825810562 |
| source | American Association for the Advancement of Science; MEDLINE |
| subjects | Kinases Protein Serine-Threonine Kinases - genetics Signal Transduction Substrates |
| title | Capturing conformational transitions of full-length PDK1 that dictate kinase substrate selectivity |
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