1ZOE

Crystal structure of protein kinase CK2 in complex with TBB-derivatives inhibitors

1ZOE の概要

• エントリーDOI: 10.2210/pdb1zoe/pdb
• 関連するPDBエントリー: 1ZOG 1ZOH
• 分子名称: Protein kinase CK2, alpha Subunit, CHLORIDE ION, 4,5,6,7-TETRABROMO-N,N-DIMETHYL-1H-BENZIMIDAZOL-2-AMINE, ... (5 entities in total)
• 機能のキーワード: protein kinase, inhibitor, complex, transferase
• 由来する生物種: Zea mays
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39881.54

構造登録者

Battistutta, R.,Mazzorana, M.,Sarno, S.,Kazimierczuk, Z.,Zanotti, G.,Pinna, L.A. (登録日: 2005-05-13, 公開日: 2005-11-29, 最終更新日: 2024-02-14)

主引用文献

Battistutta, R.,Mazzorana, M.,Sarno, S.,Kazimierczuk, Z.,Zanotti, G.,Pinna, L.A.
Inspecting the structure-activity relationship of protein kinase CK2 inhibitors derived from tetrabromo-benzimidazole.
Chem.Biol., 12:1211-1219, 2005

PubMed Abstract: CK2 is a very pleiotropic protein kinase whose high constitutive activity is suspected to cooperate to neoplasia. Here, the crystal structure of the complexes between CK2 and three selective tetrabromo-benzimidazole derivatives inhibiting CK2 with Ki values between 40 and 400 nM are presented. The ligands bind to the CK2 active site in a different way with respect to the parent compound TBB. They enter more deeply into the cavity, establishing halogen bonds with the backbone of Glu114 and Val116 in the hinge region. A detailed analysis of the interactions highlights a major role of the hydrophobic effect in establishing the rank of potency within this class of inhibitors and shows that polar interactions are responsible for the different orientation of the molecules in the active site.

PubMed: 16298300
DOI: 10.1016/j.chembiol.2005.08.015

実験手法

X-RAY DIFFRACTION (1.77 Å)