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Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitorsStructural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein tyrosine phosphatases (PTPs) play roles in many biological processes and are considered to be important targets for drug discovery. As inhibitor development has proven challenging, crystal structure-based design will be very helpful to advance inhibitor potency and selectivity. Successful application of protein crystallography to drug discovery heavily relies on high-quality crystal structures of the protein of interest complexed with pharmaceutically interesting ligands. It is very important to be able to produce protein-ligand crystals rapidly and reproducibly for as many ligands as necessary. This study details our efforts to engineer the catalytic domain of human protein tyrosine phosphatase beta (HPTPbeta-CD) with properties suitable for rapid-turnaround crystallography. Structures of apo HPTPbeta-CD and its complexes with several novel small-molecule inhibitors are presented here for the first time. Engineering the catalytic domain of human protein tyrosine phosphatase beta for structure-based drug discovery.,Evdokimov AG, Pokross M, Walter R, Mekel M, Cox B, Li C, Bechard R, Genbauffe F, Andrews R, Diven C, Howard B, Rastogi V, Gray J, Maier M, Peters KG Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1435-45. Epub 2006, Nov 23. PMID:17139078[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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