Crystal structure of the SALL4-pomalidomide-cereblon-DDB1 complex.
Nat Struct Mol Biol. 2020 Apr;27(4):319-322. Epub 2020 Apr 06
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摘要
Thalidomide-dependent degradation of the embryonic transcription factor SALL4 by the CRL4CRBN E3 ubiquitin ligase is a plausible major driver of thalidomide teratogenicity. The structure of the second zinc finger of SALL4 in complex with pomalidomide, cereblon and DDB1 reveals the molecular details of recruitment. Sequence differences and a shifted binding position relative to Ikaros offer a path to the rational design of cereblon-binding drugs with reduced teratogenic risk.
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原始数据
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文献解读
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