Karmee, J
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The K122 loop of wild-type PTPN2 adopts a completely different conformation C216S - phosphatase-dead mutant of TCPTP C227S - site-directed mutagenesis, catalytically inactive mutant comprising residues 1-294, specific interaction between the Lyp substrate-trapping mutant and SKAP-HOM C231S - phosphatase-dead mutant of PEST C258M - isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition C270A inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339) C270S inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339) C270S/T106D inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339) C377S catalytically inactive Cdc25C C433S - phosphatase-dead mutant of PTPalpha C455S crystallization data C459S - substrate-trapping mutant of SHP2 C473D active site mutant, weak substrate affinity and dissociates rapidly C473S strong substrate affinity and dissociates slowly C488S catalytically inactive Cdc25B C92A site-directed mutagenesis, affects inhibition by abietic acid and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid C945S - site-directed mutagenesis of the essential cysteine residue to a serine in the islet cell antigen-related PTP results in the expression of the intracellular region which does not catalyze hydrolysis of 4-nitrophenyl phosphate D195A/C227S - optimized substrate-trap mutant, used for identification of physiological enzyme substrates D236A substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339), shows 420fold reduced activity compared to the wild type enzyme D236A/C270A/Q314A inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339) D236A/C270S/Q314A inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339) D236A/Q314A substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339), shows 1255fold reduced activity compared to the wild type enzyme D284A - catalytically inactive, no significant effect on proliferation in human umbilical vein endothelial cells D48N - isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition D61G - the mutation causes hyperactivation of the SHP2 catalytic activity D811A/C842S site-directed mutagenesis, analysis of binding structure of substrate Eps15846-854 compared to wild-type enzyme and enzyme PTP1B D811A/H812F/C842S/M883G site-directed mutagenesis, analysis of binding structure of substrate Eps15846-854 compared to wild-type enzyme and enzyme PTP1B
