Polo-like kinase 1–inhibitor co-complex structures via the surface-entropy reduction approach and a DARPin-assisted approach

Eberspaecher, U.; Schmitz, A.A.; Siemeister, G.; Bömer, U.; Bandeiras, T.M.; Matias, P.M.; Schulze, V.K.; Hillig, R.C.

doi:10.1107/S2059798325009325

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 7
The DARPin binding epitope covers the nuclear localization signal (NLS) of PLK1. The DARPin complex of PLK1^WT in complex with compound 1 is shown (PDB entry 9r8b; chains A and C, with PLK1 as a grey surface, the DARPin in blue ribbon representation and compound 1 in stick representation with yellow C atoms). The residues ¹³⁴RRR¹³⁶ and ¹⁴³KRRK¹⁴⁶ of the NLS sequence are highlighted as green surface patches. This NLS epitope also comprises residue Arg144 which, in the SER approach, is engaged in the crystal contact formed with the SER point mutation K225D.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 81| Part 12| December 2025| Pages 718-733

https://doi.org/10.1107/S2059798325009325

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