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TitleStructure of the CUL1-RBX1-SKP1-FBXO4 SCF ubiquitin ligase complex.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 735, Page 150811, Year 2024
Publish dateNov 26, 2024
AuthorsWenjie Zhu / Xinyan Chen / Jiahai Zhang / Chao Xu /
PubMed AbstractCullin-RING E3 ubiquitin ligases (CRLs) constitute the largest family of ubiquitin ligase and play important roles in regulation of proteostasis. Here we presented the cryo-EM structure of CRL1, a ...Cullin-RING E3 ubiquitin ligases (CRLs) constitute the largest family of ubiquitin ligase and play important roles in regulation of proteostasis. Here we presented the cryo-EM structure of CRL1, a member of Cullin-1 E3 ligase. CRL1 adopts a homodimer architecture. Structural analysis revealed that in the CRL1 protomer, the substrate recognition subunit FBXO4 interacts both the adaptor protein SKP1, and the scaffold protein CUL1 via hydrophobic and electrostatic interactions. Two FBXO4 forms a domain-swapped dimer in the CRL1 structure, which constitutes the basis for the dimerization of CRL1. Inspired by the cryo-EM density, we modeled the architecture of whole CRL1 as a symmetrical dimer, which provides insights into CRL1-medaited turnover of oncogene proteins.
External linksBiochem Biophys Res Commun / PubMed:39406020
MethodsEM (single particle)
Resolution3.93 Å
Structure data

EMDB-61550: Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO4 SCF ubiquition ligase complex
Method: EM (single particle) / Resolution: 3.93 Å

Source
  • Homo sapiens (human)

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