NDLI: Gold(I) phosphine mediated selective inhibition of lymphoid tyrosine phosphatase

Content Provider	PubMed Central
Author	Karver, Mark R. Krishnamurthy, Divya Bottini, Nunzio Barrios, Amy M.
Copyright Year	2009
Abstract	Selective protein tyrosine phosphatase (PTP) inhibition is often difficult to achieve owing to the high degree of similarity of the catalytic domains of this family of enzymes. Selective inhibitors of the lymphoid specific tyrosine phosphatase, LYP, are of great interest due to the involvement of LYP in several autoimmune disorders. This manuscript describes a study into the mechanistic details of selective LYP inhibition by a Au(I)-phosphine complex. The complex, [Au((CH2CH2CN)2PPh)Cl], selectively inhibits LYP activity both in vitro and in cells, but does not inhibit other T-cell derived PTPs including the highly homologous PTP-PEST. The mode of inhibition was probed by investigating inhibition of LYP, the LYP mutant C129/231S, and PTP-PEST. Inhibition of LYP and PTP-PEST was competitive, while the LYP double mutant appeared mixed. Wild-type LYP was inhibited more potently than LYP C129/231S, indicating an important role for at least one of these residues in Au(I) binding. Coordination of Au(I) by both the active site cysteine residue as well as either Cys129 or 231 is suggested as a potential mechanism for LYP selective inhibition.
Related Links	http://dx.doi.org/10.1016/j.jinorgbio.2009.12.012
Ending Page	273
Page Count	6
Starting Page	268
File Format	PDF
ISSN	01620134
e-ISSN	18733344
Journal	Journal of inorganic biochemistry
Issue Number	3
Volume Number	104
Language	English
Publisher Date	2010-03-01
Access Restriction	Open
Subject Keyword	Inorganic Chemistry Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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