Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Dynamic molecular architecture and substrate recruitment of cullin3-RING E3 ligase CRL3.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 31, Issue 2, Page 336-350, Year 2024
Publish date	Feb 8, 2024
Authors	Yuxia Hu / Zhao Zhang / Qiyu Mao / Xiang Zhang / Aihua Hao / Yu Xun / Yeda Wang / Lin Han / Wuqiang Zhan / Qianying Liu / Yue Yin / Chao Peng / Eva Marie Y Moresco / Zhenguo Chen / Bruce Beutler / Lei Sun /
PubMed Abstract	Phosphatidylinositol 3-kinase α, a heterodimer of catalytic p110α and one of five regulatory subunits, mediates insulin- and insulin like growth factor-signaling and, frequently, oncogenesis. ...Phosphatidylinositol 3-kinase α, a heterodimer of catalytic p110α and one of five regulatory subunits, mediates insulin- and insulin like growth factor-signaling and, frequently, oncogenesis. Cellular levels of the regulatory p85α subunit are tightly controlled by regulated proteasomal degradation. In adipose tissue and growth plates, failure of K48-linked p85α ubiquitination causes diabetes, lipodystrophy and dwarfism in mice, as in humans with SHORT syndrome. Here we elucidated the structures of the key ubiquitin ligase complexes regulating p85α availability. Specificity is provided by the substrate receptor KBTBD2, which recruits p85α to the cullin3-RING E3 ubiquitin ligase (CRL3). CRL3 forms multimers, which disassemble into dimers upon substrate binding (CRL3-p85α) and/or neddylation by the activator NEDD8 (CRL3~N8), leading to p85α ubiquitination and degradation. Deactivation involves dissociation of NEDD8 mediated by the COP9 signalosome and displacement of KBTBD2 by the inhibitor CAND1. The hereby identified structural basis of p85α regulation opens the way to better understanding disturbances of glucose regulation, growth and cancer.
External links	Nat Struct Mol Biol / PubMed:38332366
Methods	EM (single particle)
Resolution	3.76 - 12.18 Å
Structure data	34199 8gq6 EMDB-34199, PDB-8gq6: Cryo-EM Structure of the KBTBD2-CUL3-Rbx1 dimeric complex Method: EM (single particle) / Resolution: 3.96 Å 34449 8h33 EMDB-34449, PDB-8h33: Cryo-EM Structure of the KBTBD2-Cul3-Rbx1 tetrameric complex Method: EM (single particle) / Resolution: 7.86 Å 34450 8h34 EMDB-34450, PDB-8h34: Cryo-EM Structure of the KBTBD2-Cul3-Rbx1 hexameric complex Method: EM (single particle) / Resolution: 7.99 Å 34451 8h35 EMDB-34451, PDB-8h35: Cryo-EM Structure of the KBTBD2-Cul3-Rbx1 octameric complex Method: EM (single particle) / Resolution: 7.41 Å 34452 8h36 EMDB-34452, PDB-8h36: Cryo-EM Structure of the KBTBD2-CUL3-Rbx1-p85a dimeric complex Method: EM (single particle) / Resolution: 4.6 Å 34453 8h37 EMDB-34453, PDB-8h37: Cryo-EM Structure of the KBTBD2-CUL3-Rbx1-p85a tetrameric complex Method: EM (single particle) / Resolution: 7.52 Å EMDB-34454: local refinement of KBTBD2-p85a: KBTBD2-CRL3-p85a complex Method: EM (single particle) / Resolution: 4.11 Å 34455 8h38 EMDB-34455, PDB-8h38: Cryo-EM Structure of the KBTBD2-CRL3~N8-CSN(mutate) complex Method: EM (single particle) / Resolution: 4.25 Å EMDB-34456: local refinement of CSN1/2/4/5/6-CRL3/CTD-N8: KBTBD2-CRL3-CSN(mutate) complex Method: EM (single particle) / Resolution: 4.84 Å EMDB-34457: local refinement of CSN1/3/5/6/7/8: KBTBD2-CRL3-CSN(mutate) complex Method: EM (single particle) / Resolution: 4.21 Å EMDB-34458: local refinement of CSN5/6-CRL3/CTD-N8: KBTBD2-CRL3-CSN(mutate) complex Method: EM (single particle) / Resolution: 4.29 Å EMDB-34459: local refinement of KBTBD2-CRL3-CSN(mutate) complex Method: EM (single particle) / Resolution: 4.25 Å EMDB-34460: Cryo-EM Structure of the KBTBD2-CRL3~N8-CSN(mutate,no CSN3/8) complex Method: EM (single particle) / Resolution: 6.83 Å EMDB-34461: Cryo-EM Structure of the KBTBD2-CRL3~N8-CSN(mutate)-CSN(mutate,no CSN3/8) complex Method: EM (single particle) / Resolution: 8.05 Å 34462 8h3a EMDB-34462, PDB-8h3a: Cryo-EM Structure of the KBTBD2-CRL3~N8(removed)-CSN complex Method: EM (single particle) / Resolution: 7.51 Å EMDB-34463: Cryo-EM Structure of the KBTBD2-CRL3~N8(removed)-CSN(no CSN3/8) complex Method: EM (single particle) / Resolution: 7.15 Å EMDB-34466: Cryo-EM Structure of the KBTBD2-CRL3-CSN(no CSN3/8) complex Method: EM (single particle) / Resolution: 12.18 Å 34467 8h3f EMDB-34467, PDB-8h3f: Cryo-EM Structure of the KBTBD2-CRL3-CSN complex Method: EM (single particle) / Resolution: 6.73 Å 34473 8h3q EMDB-34473, PDB-8h3q: Cryo-EM Structure of the CAND1-Cul3-Rbx1 complex Method: EM (single particle) / Resolution: 3.76 Å 34474 8h3r EMDB-34474, PDB-8h3r: Cryo-EM Structure of the KBTBD2-CRL3~N8 dimeric complex Method: EM (single particle) / Resolution: 6.36 Å
Chemicals	ChemComp-ZN: Unknown entry
Source	homo sapiens (human)
Keywords	LIGASE / complex