| Literature DB >> 32251415 |
Mary E Matyskiela1, Thomas Clayton2, Xinde Zheng2, Christopher Mayne2, Eileen Tran2, Aaron Carpenter2, Barbra Pagarigan2, Joseph McDonald2, Mark Rolfe2, Lawrence G Hamann2, Gang Lu2, Philip P Chamberlain3.
Abstract
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.Entities:
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Year: 2020 PMID： 32251415 DOI： 10.1038/s41594-020-0405-9
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369