4PY1

Crystal structure of Tyk2 in complex with compound 15, 6-((2,5-dimethoxyphenyl)thio)-3-(1-methyl-1H-pyrazol-4-yl)-[1,2,4]triazolo[4,3-b]pyridazine

4PY1 の概要

• エントリーDOI: 10.2210/pdb4py1/pdb
• 分子名称: Non-receptor tyrosine-protein kinase TYK2, 6-[(2,5-dimethoxyphenyl)sulfanyl]-3-(1-methyl-1H-pyrazol-4-yl)[1,2,4]triazolo[4,3-b]pyridazine (3 entities in total)
• 機能のキーワード: kinase, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36918.98

構造登録者

Han, S.,Knafels, J.D. (登録日: 2014-03-25, 公開日: 2014-09-03, 最終更新日: 2024-11-20)

主引用文献

Galatsis, P.,Henderson, J.L.,Kormos, B.L.,Han, S.,Kurumbail, R.G.,Wager, T.T.,Verhoest, P.R.,Noell, G.S.,Chen, Y.,Needle, E.,Berger, Z.,Steyn, S.J.,Houle, C.,Hirst, W.D.
Kinase domain inhibition of leucine rich repeat kinase 2 (LRRK2) using a [1,2,4]triazolo[4,3-b]pyridazine scaffold.
Bioorg.Med.Chem.Lett., 24:4132-4140, 2014

PubMed Abstract: Leucine rich repeat kinase 2 (LRRK2) has been genetically linked to Parkinson's disease (PD). The most common mutant, G2019S, increases kinase activity, thus LRRK2 kinase inhibitors are potentially useful in the treatment of PD. We herein disclose the structure, potential ligand-protein binding interactions, and pharmacological profiling of potent and highly selective kinase inhibitors based on a triazolopyridazine chemical scaffold.

PubMed: 25113930
DOI: 10.1016/j.bmcl.2014.07.052

実験手法

X-RAY DIFFRACTION (2.16 Å)