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TitleA structural basis for chaperone repression of stress signalling from the endoplasmic reticulum
Journal, issue, pagesTo Be Published
Publish dateJan 24, 2025 (structure data deposition date)
AuthorsNeidhardt L / Tung J / Ron D / Yan Y
External linksSearch PubMed
MethodsEM (single particle) / X-ray diffraction
Resolution1.9 - 4.1 Å
Structure data

52616

9i3u

EMDB-52616, PDB-9i3u:
Cryo-EM structure of the AGR2 dimer in complex with the monomeric IRE1beta luminal domain
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-52618: A cryo-EM map for two copies of IRE1beta-(AGR2)2 trimer
Method: EM (single particle) / Resolution: 4.1 Å

PDB-9i3f:
Crystal structure of the AGR2 and IRE1beta_loop complex
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsCHAPERONE / molecular chaperones / unfolded protein response (UPR) / endoplasmic reticulum (ER) / protein multimerisation / endoplasmic reticulum (ER) / molecular chaperones/ protein multimerisation/ unfolded protein response (UPR)

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