2OXY

Protein kinase CK2 in complex with tetrabromobenzoimidazole derivatives K17, K22 and K32

2OXY の概要

• エントリーDOI: 10.2210/pdb2oxy/pdb
• 関連するPDBエントリー: 1j91 1zoe 1zog 1zoh 2OXD 2OXX
• 分子名称: Casein kinase II subunit alpha, 4,5,6,7-TETRABROMO-BENZIMIDAZOLE (3 entities in total)
• 機能のキーワード: protein kinase ck2, inhibitors, tetrabromobenzoimidazole derivatives, transferase
• 由来する生物種: Zea mays
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79449.77

構造登録者

Battistutta, R.,Zanotti, G.,Cendron, L. (登録日: 2007-02-21, 公開日: 2007-09-25, 最終更新日: 2024-02-21)

主引用文献

Battistutta, R.,Mazzorana, M.,Cendron, L.,Bortolato, A.,Sarno, S.,Kazimierczuk, Z.,Zanotti, G.,Moro, S.,Pinna, L.A.
The ATP-Binding Site of Protein Kinase CK2 Holds a Positive Electrostatic Area and Conserved Water Molecules.
Chembiochem, 8:1804-1809, 2007

PubMed Abstract: CK2 is a highly pleiotropic Ser/Thr protein kinase that is able to promote cell survival and enhance the tumour phenotype under specific circumstances. We have determined the crystal structure of three new complexes with tetrabromobenzimidazole derivatives that display K(i) values between 0.15 and 0.30 microM. A comparative analysis of these data with those of four other inhibitors of the same family revealed the presence of some highly conserved water molecules in the ATP-binding site. These waters reside near Lys68, in an area with a positive electrostatic potential that is able to attract and orient negatively charged ligands. The presence of this positive region and two unique bulky residues that are typical of CK2, Ile66 and Ile174, play a critical role in determining the ligand orientation and binding selectivity.

PubMed: 17768728
DOI: 10.1002/cbic.200700307

実験手法

X-RAY DIFFRACTION (1.812 Å)