3NSZ

Human CK2 catalytic domain in complex with AMPPN

3NSZ の概要

• エントリーDOI: 10.2210/pdb3nsz/pdb
• 分子名称: Casein kinase II subunit alpha, GLYCEROL, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: kinase, ck2, inhibitor, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40358.05

構造登録者

Ferguson, A.D. (登録日: 2010-07-02, 公開日: 2010-12-15, 最終更新日: 2023-12-27)

主引用文献

Ferguson, A.D.,Sheth, P.R.,Basso, A.D.,Paliwal, S.,Gray, K.,Fischmann, T.O.,Le, H.V.
Structural basis of CX-4945 binding to human protein kinase CK2.
Febs Lett., 585:104-110, 2011

PubMed Abstract: Protein kinase CK2 (CK2), a constitutively active serine/threonine kinase, is involved in a variety of roles essential to the maintenance of cellular homeostasis. Elevated levels of CK2 expression results in the dysregulation of key signaling pathways that regulate transcription, and has been implicated in cancer. The adenosine-5'-triphosphate-competitive inhibitor CX-4945 has been reported to show broad spectrum anti-proliferative activity in multiple cancer cell lines. Although the enzymatic IC(50) of CX-4945 has been reported, the thermodynamics and structural basis of binding to CK2α remained elusive. Presented here are the crystal structures of human CK2α in complex with CX-4945 and adenylyl phosphoramidate at 2.7 and 1.3 Å, respectively. Biophysical analysis of CX-4945 binding is also described. This data provides the structural rationale for the design of more potent inhibitors against this emerging cancer target.

PubMed: 21093442
DOI: 10.1016/j.febslet.2010.11.019

実験手法

X-RAY DIFFRACTION (1.3 Å)