Discovery and Structural Characterization of Small Molecule Binders of the Human CTLH E3 Ligase Subunit GID4
Chetan K. Chana, Pierre Maisonneuve, Ganna Posternak, Nicolas G.A. Grinberg, Juline Poirson, Samara Mishelle Ona, Derek F. Ceccarelli, P. Mäder, Daniel J. St‐Cyr, Victor P.T. Pau, Igor Kurinov, Xiaojing Tang, Dongjing Deng, Weiren Cui, Wenji Su, Letian Kuai, Richard Söll, Mike Tyers, Hannes Röst, Robert A. Batey, Mikko Taipale, Anne‐Claude Gingras, Frank Sicheri
Abstract
of 558 nM in cells with strong selectivity for GID4. X-ray co-structure determination revealed the basis for GID4-small molecule interactions. These results position GID4-CTLH as an E3 for TPD and provide candidate scaffolds for high-affinity moieties that bind GID4.
Topics & Concepts
ChemistryUbiquitin ligaseProtein subunitSmall moleculeDNA ligaseStereochemistryIn vitroUbiquitinMoleculeEffectorUbiquitin-Protein LigasesBiochemistryBiophysicsDNAGeneBiologyOrganic chemistryProtein Degradation and InhibitorsUbiquitin and proteasome pathwaysPeptidase Inhibition and Analysis