6HK6

Human RIOK2 bound to inhibitor

Summary for 6HK6

• Entry DOI: 10.2210/pdb6hk6/pdb
• Descriptor: Serine/threonine-protein kinase RIO2, 2-naphthalen-2-yl-~{N}-pyridin-2-yl-ethanamide, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: kinase, structural genomics consortium, sgc, transferase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 10
• Total formula weight: 386800.42

Authors

Wang, J.,Krojer, T.,Bountra, C.,Edwards, A.M.,Arrowsmith, C.,Knapp, S.,Elkins, J.M. (deposition date: 2018-09-05, release date: 2018-10-24, Last modification date: 2024-01-17)

Primary citation

Wang, J.,Varin, T.,Vieth, M.,Elkins, J.M.
Crystal structure of human RIOK2 bound to a specific inhibitor.
Open Biology, 9:190037-190037, 2019

PubMed Abstract: 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.

PubMed: 30991936
DOI: 10.1098/rsob.190037

Experimental method

X-RAY DIFFRACTION (2.35 Å)