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dc.contributor.authorSkinner, Andria L.
dc.contributor.authorLaurence, Jennifer S.
dc.date.accessioned2017-04-28T20:36:45Z
dc.date.available2017-04-28T20:36:45Z
dc.date.issued2009-06
dc.identifier.citationSkinner, A. L., & Laurence, J. S. (2009). 1H, 15N, 13C Resonance Assignments of the Reduced and Active Form of Human Protein Tyrosine Phosphatase, PRL-1. Biomolecular NMR Assignments, 3(1), 61–65. http://doi.org/10.1007/s12104-008-9142-4en_US
dc.identifier.urihttp://hdl.handle.net/1808/23860
dc.description.abstractPhosphatase of regenerating liver-1 (PRL-1) is a novel target for potentially treating cancer metastases. Although its specific biochemical role in these processes has yet to be delineated, considerable evidence suggests the phosphatase activity of PRL-1 is required for promoting cancer and metastasis. PRL-1 belongs to the protein tyrosine phosphatase (PTPase) family and functions using the CX5R consensus active site motif. Like other PTPases, PRL-1 is inhibited by oxidation at its active site Cys, however, disulfide bond formation occurs unusually readily in wild-type PRL-1. Chemical shift assignments are available for oxidized wild type, but numerous, substantial changes are observed in the spectra upon reduction. Because the reduced form is active, we sought to identify a stable mutant that would resist oxidation and be useful for facilitating drug screening and development using NMR-based assays. We present here NMR assignments for a full-length, reduced and active form of PRL-1, PRL-1-C170S-C171S, that is well suited for this purpose.en_US
dc.publisherSpringer Verlagen_US
dc.rights© Springer Science+Business Media B.V. 2009en_US
dc.title1H, 15N, 13C Resonance Assignments of the Reduced and Active Form of Human Protein Tyrosine Phosphatase, PRL-1en_US
dc.typeArticleen_US
kusw.kuauthorSkinner, Andria L.
kusw.kuauthorLaurence, Jennifer S.
kusw.kudepartmentPharmaceutical Chemistryen_US
dc.identifier.doi10.1007/s12104-008-9142-4en_US
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.identifier.pmidPMC2719816en_US
dc.rights.accessrightsopenAccess


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