A promiscuous kinase inhibitor delineates the conspicuous structural features of protein kinase CK2a1. Issue 7 (8th July 2019)

• Record Type: Journal Article
• Authors: Tsuyuguchi, Masato; Nakaniwa, Tetsuko; Sawa, Masaaki; Nakanishi, Isao; Kinoshita, Takayoshi
• Is Part Of: Acta crystallographica. Volume 75:Issue 7(2019:Jul.)
• Page Start: 515
• Page End: 519
• Publication Date: 2019-07-08
• Subjects: protein kinase CK2 -- ATP‐analogue inhibitor -- selectivity -- off‐target kinases -- structural comparison; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X19008951
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The crystal structure of protein kinase CK2a1 in complex with 5‐iodotubercidin, an ATP‐analogue inhibitor, was determined at 1.78 Å resolution. This structure should facilitate the discovery of selective CK2a1 inhibitors. Abstract : Protein kinase CK2a1 is a serine/threonine kinase that plays a crucial role in the growth, proliferation and survival of cells and is a well known target for tumour and glomerulonephritis therapies. Here, the crystal structure of the kinase domain of CK2a1 complexed with 5‐iodotubercidin (5IOD), an ATP‐mimetic inhibitor, was determined at 1.78 Å resolution. The structure shows distinct structural features and, in combination with a comparison of the crystal structures of five off‐target kinases complexed with 5IOD, provides valuable information for the development of highly selective inhibitors.