6uml

Structural Basis for Thalidomide Teratogenicity Revealed by the Cereblon-DDB1-SALL4-Pomalidomide Complex

spinqualitylabelsall models 6uml, resolution 3.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.58Å Ligands: Y70, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Thalidomide-dependent degradation of the embryonic transcription factor SALL4 by the CRL4(CRBN) 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. Crystal structure of the SALL4-pomalidomide-cereblon-DDB1 complex.,Matyskiela ME, Clayton T, Zheng X, Mayne C, Tran E, Carpenter A, Pagarigan B, McDonald J, Rolfe M, Hamann LG, Lu G, Chamberlain PP Nat Struct Mol Biol. 2020 Apr;27(4):319-322. doi: 10.1038/s41594-020-0405-9. Epub, 2020 Apr 6. PMID:32251415 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DNA damage-binding protein

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