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TitleOligomer-to-monomer transition underlies the chaperone function of AAGAB in AP1/AP2 assembly.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 120, Page e2205199120-e2205199120, Year 2023
Publish dateFeb 7, 2022 (structure data deposition date)
AuthorsTian, Y. / Datta, I. / Yang, R. / Wan, C. / Wang, B. / Crisman, L. / He, H. / Brautigam, C.A. / Li, S. / Shen, J. / Yin, Q.
External linksProc. Natl. Acad. Sci. USA / PubMed:36598941
MethodsX-ray diffraction
Resolution2.11 Å
Structure data

PDB-7twd:
Structure of AAGAB C-terminal dimerization domain
Method: X-RAY DIFFRACTION / Resolution: 2.11 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsCHAPERONE / protein binding / membrane trafficking / AP Complex

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