› 3loz

X-ray diffraction
1.8Å resolution

Crystal structure of Beta 2 Microglobulin amyloidogenic segment LSFSKD

Released:
DOI: 10.2210/pdb3loz/pdb
PDB entry 3loz coloured by chain, front view.
PDB entry 3loz coloured by chain, side view.
PDB entry 3loz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.
Liu C, Sawaya MR, Eisenberg D
Nat Struct Mol Biol 18 49-55 (2011)
PMID: 21131979

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158383 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-2-microglobulin form pI 5.3 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 6 amino acids
Theoretical weight: 697 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P61769 (Residues: 74-79; Coverage: 6%)
Gene names: B2M, CDABP0092, HDCMA22P

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 9.425Å b: 21.482Å c: 45.731Å
α: 90° β: 90.02° γ: 90°
R-values:
R R work R free
0.219 0.216 0.241
Expression system: Not provided

Quick links

Citations

15 review citations

A diversity of assembly mechanisms of a generic amyloid fold.
Eichner et al. (2011)
14 more

8 mentions without citation

β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.
Liu et al. (2011)
7 more