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TitleStructures of Fab-stabilized CHIP reveal a conformational switch important in E3 ligase and chaperone functions
Journal, issue, pagesTo Be Published
Publish dateApr 15, 2025 (structure data deposition date)
AuthorsUnnikrishnan A / Southworth D
External linksSearch PubMed
MethodsEM (single particle)
Resolution3.1 - 4.8 Å
Structure data

70196

9o7e

EMDB-70196, PDB-9o7e:
CHIP E3 ligase dimer in intermediate state bound to 2 Fab H1
Method: EM (single particle) / Resolution: 3.9 Å

70198

9o7g

EMDB-70198, PDB-9o7g:
CHIP E3 ligase U-box-Fab H1 epitope focused refinement
Method: EM (single particle) / Resolution: 3.1 Å

70199

9o7h

EMDB-70199, PDB-9o7h:
CHIP E3 ligase dimer bound to 1 Fab 2D2
Method: EM (single particle) / Resolution: 4.8 Å

70200

9o7i

EMDB-70200, PDB-9o7i:
CHIP E3 ligase CC domain dimer-Fab 2D2 epitope focused refinement
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • homo sapiens (human)
KeywordsLIGASE/IMMUNE SYSTEM / U-box E3 ligase / Fab / Cryo-EM / Protein degradation / LIGASE-IMMUNE SYSTEM complex

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