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 4
Binding mode of thiazolidinone compound 1 soaked into a crystal of PLK1^WT:DARPin. (a) Overall view of the complex of the kinase domain of PLK1^WT (grey ribbon representation), the DARPin molecule (blue ribbon representation) and compound 1 (stick representation, C atoms in green). Heterodimer 1 (chains A and C) of the two dimers in the asymmetric unit is shown (PDB entry 9r8b). (b) 2F_o − F_c density map contoured at 1.3σ, with Cys133 in the hinge of PLK1 and the DARPin residues Asp77, Val78 and Met111 (in contact with the ligand) shown in stick representation. Hydrogen bonds are shown as dotted yellow lines. (c) Overlay of the binding modes of compound 1 from the SER approach (chain A, yellow C atoms) and from the DARPin approach (chain A, green C atoms), obtained by superimposition of the respective protein chains.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798325009325

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