1DAW

CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPHA-SUBUNIT) AND MG-AMPPNP

1DAW の概要

• エントリーDOI: 10.2210/pdb1daw/pdb
• 関連するPDBエントリー: 1A6O 1DAY
• 分子名称: PROTEIN KINASE CK2, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: protein kinase ck2, dual-cosubstrate specificity, binary 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: 39228.20

構造登録者

Niefind, K.,Puetter, M.,Guerra, B.,Issinger, O.G.,Schomburg, D. (登録日: 1999-11-01, 公開日: 2000-05-03, 最終更新日: 2023-08-09)

主引用文献

Niefind, K.,Putter, M.,Guerra, B.,Issinger, O.G.,Schomburg, D.
GTP plus water mimic ATP in the active site of protein kinase CK2.
Nat.Struct.Biol., 6:1100-1103, 1999

PubMed Abstract: The structures of the catalytic subunit of protein kinase CK2 from Zea mays complexed with Mg2+ and with analogs of ATP or GTP were determined to 2.2 A resolution. Unlike most other protein kinases, CK2 from various sources shows 'dual-cosubstrate specificity', that is, the ability to efficiently use either ATP or GTP as a cosubstrate. The structures of these complexes demonstrate that water molecules are critical to switch the active site of CK2 from an ATP- to a GTP-compatible state. An understanding of the structural basis of dual-cosubstrate specificity may help in the design of drugs that target CK2 or other kinases with this property.

PubMed: 10581548
DOI: 10.1038/70033

実験手法

X-RAY DIFFRACTION (2.2 Å)