5YF9
Crystal structure of CK2a2 form-2
Summary for 5YF9
| Entry DOI | 10.2210/pdb5yf9/pdb |
| Descriptor | Casein kinase II subunit alpha', NICOTINIC ACID, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 81334.69 |
| Authors | Tsuyuguchi, M.,Kinoshita, T. (deposition date: 2017-09-20, release date: 2018-05-16, Last modification date: 2023-11-22) |
| Primary citation | Tsuyuguchi, M.,Nakaniwa, T.,Kinoshita, T. Crystal structures of human CK2 alpha 2 in new crystal forms arising from a subtle difference in salt concentration Acta Crystallogr F Struct Biol Commun, 74:288-293, 2018 Cited by PubMed Abstract: 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. PubMed: 29717996DOI: 10.1107/S2053230X18005204 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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