TJ proteins are closest to the apical membrane and seal the BBB, thus acting as potential therapeutic targets
[DOI] [PMC free article] [PubMed] [Google Scholar] 109.Kim J.E., Yoon B.A., Kim Y.H., Kim J.K., Bae J.S
It is designed to be a neutral vehicle that preserves the peptide solution without interfering with its structure or function, provided storage protocols are followed
The R221G mutation introduces a small noncharged glycine residue that, contrary to the Arg residue cannot form ionic or H-bonds and cannot interact with the WPD-loop Trp179 and Pro180 residues R33A - decreased activity R362K - the Shp2 mutant shows a strongly decreased affinity for the inhibitor phenylhydrazonopyrazolone sulfonate 1 R47V - isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition R47V/D48N/M258C/G259Q molecular dynamics simulations of the crystal structure, in comparison to wild-type, movement of Q262 is restricted R492L hotspot mutant, dramatically decreased activity despite showing no significant changes in crystal structure S19A site-directed mutagenesis, mutant PTPN12-S19A is efficient in inhibiting EGF-induced cell migration, the mutant does not produce significant differences in PTPN12's recognition of all HER2-phospho-peptides compared to wild-type PTPN12 S19E site-directed mutagenesis, mutant PTPN12-S19E is less efficient in inhibiting EGF-induced cell migration, the mutant does not produce significant differences in PTPN12's recognition of all HER2-phospho-peptides compared to wild-type PTPN12 S270A site-directed mutagenesis, mutation of the catalytic residue in the phosphatase domain, the mutant shows altered enzyme activity kinetic profiles with a synthetic small molecule substrate (pNPP) and the physiological relevant substrate (pERK) when compared to wild-type GST-DUSP5 protein
Y.WilliamsC.LibyK.et al (2010)
