4MD8

Crystal Structure of full-length symmetric CK2 holoenzyme with mutated alpha subunit (F121E)

4MD8 の概要

• エントリーDOI: 10.2210/pdb4md8/pdb
• 関連するPDBエントリー: 4MD7 4MD9
• 分子名称: Casein kinase II subunit beta, Casein kinase II subunit alpha, ZINC ION (3 entities in total)
• 機能のキーワード: protein serine/threonine kinase, transferase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 280901.27

構造登録者

Lolli, G.,Ranchio, A.,Battistutta, R. (登録日: 2013-08-22, 公開日: 2013-11-20, 最終更新日: 2023-09-20)

主引用文献

Lolli, G.,Ranchio, A.,Battistutta, R.
Active Form of the Protein Kinase CK2 alpha 2 beta 2 Holoenzyme Is a Strong Complex with Symmetric Architecture.
Acs Chem.Biol., 9:366-371, 2014

PubMed Abstract: CK2 is a protein kinase essential for cell viability whose activity is altered in several cancers. Its mechanisms of regulation differ from those common to other eukaryotic protein kinases and are not entirely established yet. Here we present crystal structures of the monomeric form of the α2β2 holoenzyme that allow refining a formerly proposed structural model for activity regulation by oligomerization. Previous crystal structures of the CK2 holoenzyme show an asymmetric arrangement of the two α catalytic subunits around the obligate β2 regulatory subunits. Asymmetric α2β2 tetramers are organized in trimeric rings that correspond to inactive forms of the enzyme. The new crystal structures presented here reveal the symmetric architecture of the isolated active tetramers. The dimension and the nature of the α/β interfaces configure the holoenzyme as a strong complex that does not spontaneously dissociate in solution, in accordance with the low dissociation constant (∼4 nM).

PubMed: 24175891
DOI: 10.1021/cb400771y

実験手法

X-RAY DIFFRACTION (3.3 Å)