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A promiscuous kinase inhibitor delineates the conspicuous structural features of protein kinase CK2a1.
Acta Crystallographica Section F ( IF 1.072 ) Pub Date : 2019-07-08 , DOI: 10.1107/s2053230x19008951
Masato Tsuyuguchi 1 , Tetsuko Nakaniwa 2 , Masaaki Sawa 3 , Isao Nakanishi 4 , Takayoshi Kinoshita 1
Affiliation  

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.

中文翻译:

混杂的激酶抑制剂描述了蛋白激酶CK2a1的明显结构特征。

蛋白激酶CK2a1是一种丝氨酸/苏氨酸激酶,在细胞的生长,增殖和存活中起关键作用,并且是肿瘤和肾小球肾炎治疗的众所周知的靶标。在这里,以1.78Å的分辨率测定了与ATP抑制物5-碘苯哌丁啶(5IOD)配合的CK2a1激酶结构域的晶体结构。该结构显示出独特的结构特征,并与五个与5IOD复合的脱靶激酶的晶体结构进行比较,为开发高选择性抑制剂提供了有价值的信息。
更新日期:2019-07-08
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