3she | pdb_00003she

Novel ATP-competitive MK2 inhibitors with potent biochemical and cell-based activity throughout the series

spinqualitylabelsall models 3she, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3she is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: I85 Gene: MAPKAPK3 (Homo sapiens) Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Optimization of our previously described pyrrolopiperidone series led to the identification of a new benzamide sub-series, which exhibits consistently high potency in biochemical and cell-based assays throughout the series. Strong inhibition of LPS-induced production of the cytokine TNFalpha is coupled to the regulation of HSP27 phosphorylation, indicating that the observed cellular effects result from the inhibition of MK2. X-ray crystallographic and computational analyses provide a rationale for the high potency of the series. Novel ATP competitive MK2 inhibitors with potent biochemical and cell-based activity throughout the series.,Oubrie A, Kaptein A, de Zwart E, Hoogenboom N, Goorden R, van de Kar B, van Hoek M, de Kimpe V, van der Heijden R, Borsboom J, Kazemier B, de Roos J, Scheffers M, Lommerse J, Schultz-Fademrecht C, Barf T Bioorg Med Chem Lett. 2011 Nov 3. PMID:22119462 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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