Potent Low Molecular Weight Substrates for Protein-tyrosine Phosphatase
نویسندگان
چکیده
منابع مشابه
Solution structure of a low molecular weight protein tyrosine phosphatase.
Protein tyrosine phosphatases (PTPs) are important enzymes involved in signal transduction, cell cycle regulation, and the control of differentiation. Despite the importance of this class of enzymes in the control of critical cell processes, very little structural information is available for this family of proteins. In this paper, we present the first solution structure of a protein tyrosine p...
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Herein, we provide new contribution to the mechanisms involved in keratinocytes response to hyperosmotic shock showing, for the first time, the participation of Low Molecular Weight Protein Tyrosine Phosphatase (LMWPTP) activity in this event. We reported that sorbitol-induced osmotic stress mediates alterations in the phosphorylation of pivotal cytoskeletal proteins, particularly Src and cofil...
متن کاملCrystal structure of low-molecular-weight protein tyrosine phosphatase from Mycobacterium tuberculosis at 1.9-A resolution.
The low-molecular-weight protein tyrosine phosphatase (LMWPTPase) belongs to a distinctive class of phosphotyrosine phosphatases widely distributed among prokaryotes and eukaryotes. We report here the crystal structure of LMWPTPase of microbial origin, the first of its kind from Mycobacterium tuberculosis. The structure was determined to be two crystal forms at 1.9- and 2.5-A resolutions. These...
متن کاملCharacterization of low molecular weight protein tyrosine phosphatase isoforms in human breast cancer epithelial cell lines.
BACKGROUND Low molecular weight protein tyrosine phosphatase (LMW-PTP) is a polymorphic protein with two major isoforms whose role in tumorigenesis is currently controversial. MATERIALS AND METHODS We characterized LMW-PTP genotype, isoform expression and activity in six different human breast cancer epithelial cell lines (ZR75, MDA-MB-231, MDA-MB-231BO, MCF7, MDA-MB-231BO2, MDA-MB-435) and c...
متن کاملHydrogen-bonding interactions in the active site of a low molecular weight protein-tyrosine phosphatase
Molecular dynamics simulation of the Michaelis complex, phospho-enzyme intermediate, and the wild-type and C12S mutant have been carried out to examine hydrogen-bonding interactions in the active site of the bovine low molecular weight protein-tyrosine phosphatase (BPTP). It was found that the Sγ atom of the nucleophilic residue Cys-12 is ideally located at a position opposite from the phenylph...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.13.7868