Journal of Medicinal Chemistry · 2022 · 54 citations · 44 references
Life SciencesBiochemistryMolecular BiologyProtein-protein InteractionsStructural BiochemistryStructural BiologyEnzyme FunctionLigand BindingProtein Complex AssemblyProtein DegradationProtein MisfoldingProtein StructureDegradationDna-encoded Library TechnologyE3 Ubiquitin Ligase Substrate RecognitionSelectivitySubstrate DegradationTargeted Protein DegradationUbiquitin-mediated DegradationX-ray Structure Determination
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.
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Features and development of <i>Coot</i>
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<i>Phaser</i>crystallographic software
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