1H, 15N, 13C resonance assignments of the reduced and active form of human Protein Tyrosine Phosphatase, PRL-1 |
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Authors: | Andria L Skinner Jennifer S Laurence |
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Institution: | (1) Department of Pharmaceutical Chemistry, The University of Kansas, Multidisciplinary Research Building Room 356, 2030 Becker Dr, Lawrence, KS 66047, USA |
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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. |
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Keywords: | PRL-1 PTPase Resonance assignments Oxidation Reduction Redox Drug screening |
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