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Structure paper

TitleBeta2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 18, Page 49-55, Year 2011
Publish dateFeb 4, 2010 (structure data deposition date)
AuthorsLiu, C. / Sawaya, M.R. / Eisenberg, D.
External linksNat. Struct. Mol. Biol. / PubMed:21131979
MethodsX-ray diffraction
Resolution1.8 - 2.3 Å
Structure data

PDB-3low:
Crystal structure of Beta 2 Microglobulin domain-swapped dimer
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3loz:
Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / domain-swap / beta sheet hinge region / Amyloidosis / Inter-molecular disulfide bond / steric zipper / beta spine / beta 2 microglobulin

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