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• W2045621454 startingPage "5256" @default.
• W2045621454 abstract "The epidermal growth factor-derived (EGFR988) fluorophosphonate peptide, DADE(F2Pmp)L, is a potent (30 pM) inhibitor of the protein tyrosine phosphatase PTP1B. Nuclear magnetic resonance (NMR) transferred nuclear Overhauser effect (nOe) experiments have been used to determine the conformation of DADE(F2Pmp)L while bound in the active site of PTP1B. When bound, the peptide adopts an extended beta-strand conformation. Molecular modeling and molecular dynamics simulations allowed the elucidation of the sources of many of the interactions leading to binding of this inhibitor. Electrostatic, hydrophobic, and hydrogen-bonding interactions were all found to contribute significantly to its binding. However, despite the overall tight binding of this inhibitor, the N-terminal and adjacent residue of the peptide were virtually unrestrained in their motion. The major contributions to binding arose from hydrophobic interactions at the leucine and at the aromatic center, hydrogen bonding to the pro-R fluorine of the fluorophosphonomethyl group, and electrostatic interactions involving the carboxylate functionalities of the aspartate and glutamate residues. These latter two residues were found to form tight contacts with surface recognition elements (arginine and lysine) situated near the active-site cleft." @default.
• W2045621454 created "2016-06-24" @default.
• W2045621454 creator A5033038494 @default.
• W2045621454 creator A5047614339 @default.
• W2045621454 date "1999-04-01" @default.
• W2045621454 modified "2023-10-18" @default.
• W2045621454 title "Nuclear Magnetic Resonance and Restrained Molecular Dynamics Studies of the Interaction of an Epidermal Growth Factor-Derived Peptide with Protein Tyrosine Phosphatase 1B^," @default.
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• W2045621454 doi "https://doi.org/10.1021/bi9825450" @default.
• W2045621454 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10213634" @default.
• W2045621454 hasPublicationYear "1999" @default.
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