dc.contributor.author | Skinner, Andria L. | |
dc.contributor.author | Laurence, Jennifer S. | |
dc.date.accessioned | 2017-04-28T20:36:45Z | |
dc.date.available | 2017-04-28T20:36:45Z | |
dc.date.issued | 2009-06 | |
dc.identifier.citation | Skinner, 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/s12104-008-9142-4 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/23860 | |
dc.description.abstract | Phosphatase 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.publisher | Springer Verlag | en_US |
dc.rights | © Springer Science+Business Media B.V. 2009 | en_US |
dc.title | 1H, 15N, 13C Resonance Assignments of the Reduced and Active Form of Human Protein Tyrosine Phosphatase, PRL-1 | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Skinner, Andria L. | |
kusw.kuauthor | Laurence, Jennifer S. | |
kusw.kudepartment | Pharmaceutical Chemistry | en_US |
dc.identifier.doi | 10.1007/s12104-008-9142-4 | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC2719816 | en_US |
dc.rights.accessrights | openAccess | |