bioRxivBiochemistryPreprint
Human CDK5-cyclin B1 structures uncover a conserved mitotic CDK activation mechanism
Andrew S. Arvai, Ke Cong, Xiao-Feng ZhengiD, Amy Verway-CoheniD, Miaw-Sheue TsaiiD, Huy Q. NguyeniD, Albino BacollaiD, Chi-Lin TsaiiD, George A. Lantz, Alexander SpektoriD, Dipanjan ChowdhuryiD, John A. TaineriD, Aleem SyediD
Abstract
Cyclin-dependent kinase 5 (CDK5), long considered atypical and activated by non-cyclin cofactors in neurons, also functions in mitosis. To resolve its activation mechanism during mitosis, we determined the first high-resolution crystal structures of CDK5-cyclin B1 in apo and nucleotide-bound states. Contrary to AlphaFold predictions, we find CDK5 structures unexpectedly mirrors CDK1-cyclin B1 assembly and activation, establishing CDK5 as a bona fide mitotic kinase acting in parallel with CDK1.
- organism: human
- assay: protein structure
- research focus: protein structure prediction
- approach: experimental assay
- Citations
- 0
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