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-Structure paper
| タイトル | Structure of the CUL1-RBX1-SKP1-FBXO4 SCF ubiquitin ligase complex. |
|---|---|
| ジャーナル・号・ページ | Biochem Biophys Res Commun, Vol. 735, Page 150811, Year 2024 |
| 掲載日 | 2024年11月26日 |
著者 | Wenjie Zhu / Xinyan Chen / Jiahai Zhang / Chao Xu / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Biochem Biophys Res Commun / PubMed:39406020 |
| 手法 | EM (単粒子) |
| 解像度 | 3.93 Å |
| 構造データ | EMDB-61550, PDB-9jkb: |
| 由来 |
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キーワード | PROTEIN BINDING / ubiquitination E3 ligase / Cryo-EM |
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