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Cover Picture: Towards the Development of Small‐Molecule MO25 Binders as Potential Indirect SPAK/OSR1 Kinase Inhibitors (ChemBioChem 5/2017)
Author(s) -
Kadri Hachemi,
Alamri Mubarak A.,
Navratilova Iva H.,
Alderwick Luke J.,
Simpkins Nigel S.,
Mehellou Youcef
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700042
Subject(s) - kinase , phosphorylation , small molecule , chemistry , protein kinase a , biochemistry , protein serine threonine kinases , microbiology and biotechnology , biology
The cover picture shows the chemical structure of HK01, a small molecule that binds the scaffolding protein MO25 and inhibits its binding to SPAK/OSR1 kinases, which subsequently reduces their catalytic activity. Such binding is translated into reduced phosphorylation and manipulation of the activities of a series of sodium, potassium and chloride ion co‐transporters, which are normally phosphorylated by the SPAK/OSR1‐MO25 protein complex. This represents a novel approach for preventing a protein kinase from binding to its activating protein partner, indirect kinase inhibition. More information can be found in the communication by Y. Mehellou et al. on page 460 in Issue 5, 2017 (DOI: 10.1002/cbic.201600620).