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

Summary for 4PY1

• Entry DOI: 10.2210/pdb4py1/pdb
• Descriptor: 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)
• Functional Keywords: kinase, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 36918.98

Authors

Han, S.,Knafels, J.D. (deposition date: 2014-03-25, release date: 2014-09-03, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.16 Å)