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Crystal structures of human CK2α2 in new crystal forms arising from a subtle difference in salt concentration
Author(s) -
Tsuyuguchi Masato,
Nakaniwa Tetsuko,
Kinoshita Takayoshi
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18005204
Subject(s) - isozyme , crystal (programming language) , crystal structure , casein kinase 2 , resolution (logic) , high resolution , crystallography , chemistry , biology , kinase , biochemistry , enzyme , computer science , protein kinase a , artificial intelligence , mitogen activated protein kinase kinase , remote sensing , programming language , geology
The catalytic subunits of protein kinase CK2 are classified into two subtypes: CK2α1 and CK2α2. CK2α1 is an attractive drug‐discovery target for various diseases such as cancers and nephritis. CK2α2 is defined as an off‐target of CK2α1 and is a potential target in the development of male contraceptive drugs. High‐resolution crystal structures of both isozymes are likely to provide crucial clues for the design of selective inhibitors of CK2α1 and/or CK2α2. To date, several crystal structures of CK2α1 have been solved at high resolutions of beyond 1.5 Å. However, crystal structures of CK2α2 have barely achieved a low resolution of around 3 Å because of the formation of needle‐shaped crystals. In this study, new crystal forms were exploited and one provided a crystal structure of CK2α2 at 1.89 Å resolution. This result, together with the structure of CK2α1, will assist in the development of highly selective inhibitors for both isozymes.