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New routes for PTP1B allosteric inhibition by multitemperature crystallography, fragment screening and covalent tethering
[article]
2017
bioRxiv
pre-print
Allostery is an inherent feature of proteins and provides alternative routes to regulating function. Small-molecule allosteric inhibitors are often desirable; however, it remains challenging to identify surface sites in proteins which can bind small molecules and modulate function. We identified new allosteric sites in protein tyrosine phosphatase 1B (PTP1B) by combining multiple-temperature X-ray crystallography experiments and structure determination from hundreds of individual small-molecule
doi:10.1101/218966
fatcat:bll5xbamebhbtlxn7oq65xa4li