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Fig. 3 | SpringerPlus

Fig. 3

From: In silico analysis of enantioselective binding of immunomodulatory imide drugs to cereblon

Fig. 3

β10–β11 hairpin of cereblon could contribute to enantiomeric selectivity and the increased affinity with IMiDs. a Docking poses of (S)-thalidomide (green) and (R)-thalidomide (cyan) using the type B structure (white). b Superimposition of the complex shown in a with the type A structure (magenta). c Docking poses of (S)-thalidomide (magenta) using the type A structure and (S)-thalidomide (green) using the type B structure. β10–β11 hairpin and the three tryptophan residues of the aromatic cage (W380, W386, and W400) of type A cereblon are shown in magenta and orange, respectively. Thalidomide, lenalidomide, and pomalidomide are described in ‘thal’, ‘len’, ‘pom’ for short, respectively

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