3db8
Crystal structure of an activated (Thr->Asp) Polo-like kinase 1 (Plk1) catalytic domain in complex with Compound 041Crystal structure of an activated (Thr->Asp) Polo-like kinase 1 (Plk1) catalytic domain in complex with Compound 041
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA series of 2-amino-isoxazolopyridines was designed and synthesized as Polo-like kinase (Plk) inhibitors. Key SAR and crystallographic data are discussed. More advanced analogues inhibit Plk1 with good enzymatic activity and modest cell-based activity. Differential selectivity among the three Plk isoforms is observed. Design and synthesis of 2-amino-isoxazolopyridines as Polo-like kinase inhibitors.,Hanan EJ, Fucini RV, Romanowski MJ, Elling RA, Lew W, Purkey HE, VanderPorten EC, Yang W Bioorg Med Chem Lett. 2008 Oct 1;18(19):5186-9. Epub 2008 Aug 29. PMID:18790636[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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