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Inhibition of protein tyrosine phosphatases PTP1B and CD45 by sulfotyrosyl peptides.

Abstract：

:Sulfotyrosyl peptides corresponding to the known high-affinity substrate phosphotyrosyl peptide sequences in casein and the autophosphorylation sites of insulin receptor and EGF receptor were investigated as inhibitors of protein tyrosine phosphatases PTP1B and CD45. These peptides inhibit both PTP1B and CD45 in the micromolar range competitively and reversibly. The elements required for inhibition were investigated by truncation and substitution of these peptides. Acidic residues N-terminal to the sulfotyrosyl residues are essential for high-affinity binding to PTP1B. The recognition elements required for inhibition of PTP1B and CD45 are different and this suggests the possibility of identifying selective active-site-directed inhibitors for these enzymes.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Desmarais S,Jia Z,Ramachandran C

doi

10.1006/abbi.1998.0691

subject

Has Abstract

pub_date

1998-06-15 00:00:00

pages

225-31

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(98)90691-9

journal_volume

354

pub_type

杂志文章

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