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The RIO kinases (RIOKs) are a universal family of atypical kinases that are essential for assembly of the pre-40S ribosome complex. Here, we present the crystal structure of human RIO kinase 2 (RIOK2) bound to a specific inhibitor. This first crystal structure of an inhibitor-bound RIO kinase reveals the binding mode of the inhibitor and explains the structure-activity relationship of the inhibitor series. The inhibitor binds in the ATP-binding site and forms extensive hydrophobic interactions with residues at the entrance to the ATP-binding site. Analysis of the conservation of active site residues reveals the reasons for the specificity of the inhibitor for RIOK2 over RIOK1 and RIOK3, and it provides a template for inhibitor design against the human RIOK family.

Original publication

DOI

10.1098/rsob.190037

Type

Journal article

Journal

Open biology

Publication Date

04/2019

Volume

9

Addresses

1 Structural Genomics Consortium, Nuffield Department of Clinical Medicine, University of Oxford , Old Road Campus Research Building, Roosevelt Drive, Oxford OX3 7DQ , UK.

Keywords

Humans, Protein-Serine-Threonine Kinases, Protein Kinase Inhibitors, Crystallography, X-Ray, Binding Sites, Molecular Structure, Catalytic Domain, Protein Conformation, Protein Binding, Structure-Activity Relationship