3KF7

Crystal Structure of Human p38alpha Complexed With a Triazolopyrimidine compound

Summary for 3KF7

• Entry DOI: 10.2210/pdb3kf7/pdb
• Descriptor: Mitogen-activated protein kinase 14, 3-{6-[2-(2,4-difluorophenyl)ethyl][1,2,4]triazolo[4,3-a]pyridin-3-yl}-4-methylbenzamide (3 entities in total)
• Functional Keywords: two lobes, atp pocket, peptide flip, atp-binding, kinase, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : Q16539
• Total number of polymer chains: 1
• Total formula weight: 41735.60

Authors

Shieh, H.-S.,Williams, J.M.,Stegeman, R.A.,Xing, L.,Jerome, K.D. (deposition date: 2009-10-27, release date: 2009-12-29, Last modification date: 2024-02-21)

Primary citation

Jerome, K.D.,Rucker, P.V.,Xing, L.,Shieh, H.S.,Baldus, J.E.,Selness, S.R.,Letavic, M.A.,Braganza, J.F.,McClure, K.F.
Continued exploration of the triazolopyridine scaffold as a platform for p38 MAP kinase inhibition.
Bioorg.Med.Chem.Lett., 20:469-473, 2010

PubMed Abstract: The structure based drug design, synthesis and structure-activity relationship of a series of C6 sulfur linked triazolopyridine based p38 inhibitors are described. The metabolic deficiencies of this series were overcome through changes in the C6 linker from sulfur to methylene, which was predicted by molecular modeling to be bioisosteric. X-ray of the ethylene linked compound 61 confirmed the predicted binding orientation of the scaffold in the p38 enzyme.

PubMed: 19969459
DOI: 10.1016/j.bmcl.2009.11.114

Experimental method

X-RAY DIFFRACTION (2 Å)