3EHA

Crystal structure of death associated protein kinase complexed with AMPPNP

3EHA の概要

• エントリーDOI: 10.2210/pdb3eha/pdb
• 関連するPDBエントリー: 1EH9 1JKK 1JKL 1JKS 1ig1
• 分子名称: Death-associated protein kinase 1, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
• 機能のキーワード: kinase domain s/t kinase, ank repeat, apoptosis, atp-binding, calmodulin-binding, cytoplasm, kinase, nucleotide-binding, phosphoprotein, polymorphism, serine/threonine-protein kinase, transferase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm: P53355
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34300.56

構造登録者

McNamara, L.K.,Watterson, D.M.,Brunzelle, J.S. (登録日: 2008-09-11, 公開日: 2009-04-28, 最終更新日: 2023-08-30)

主引用文献

McNamara, L.K.,Watterson, D.M.,Brunzelle, J.S.
Structural insight into nucleotide recognition by human death-associated protein kinase.
Acta Crystallogr.,Sect.D, 65:241-248, 2009

PubMed Abstract: Death-associated protein kinase (DAPK) is a member of the Ca(2+)/calmodulin-regulated family of serine/threonine protein kinases. The role of the kinase activity of DAPK in eukaryotic cell apoptosis and the ability of bioavailable DAPK inhibitors to rescue neuronal death after brain injury have made it a drug-discovery target for neurodegenerative disorders. In order to understand the recognition of nucleotides by DAPK and to gain insight into DAPK catalysis, the crystal structure of human DAPK was solved in complex with ADP and Mg(2+) at 1.85 A resolution. ADP is a product of the kinase reaction and product release is considered to be the rate-limiting step of protein kinase catalytic cycles. The structure of DAPK-ADP-Mg(2+) was compared with a newly determined DAPK-AMP-PNP-Mg(2+) structure and the previously determined apo DAPK structure (PDB code 1jks). The comparison shows that nucleotide-induced changes are localized to the glycine-rich loop region of DAPK.

PubMed: 19237746
DOI: 10.1107/S0907444908043679

実験手法

X-RAY DIFFRACTION (1.6 Å)