ArticleOpen biology2019
Crystal structure of human RIOK2 bound to a specific inhibitor.
Article in Open biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Exploration of tricyclic heterocycles as core structures for RIOK2 inhibitors.RSC medicinal chemistry · 2023Article
- Article
- Pan-cancer analyses reveal multi-omics and clinical characteristics of RIO kinase 2 in cancer.Frontiers in chemistry · 2022Article
- Identification of RIOK2 as a master regulator of human blood cell development.Nature immunology · 2022Article
- Towards a RIOK2 chemical probe: cellular potency improvement of a selective 2-(acylamino)pyridine series.RSC medicinal chemistry · 2021Article
- Anticancer Activities and Mechanism of Action of Nagilactones, a Group of Terpenoid Lactones Isolated from Podocarpus Species.Natural products and bioprospecting · 2020Review
- In vitro dimerization of human RIO2 kinase.RNA biology · 2019Article
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
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.
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Registered trials
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