› 2xku

Solution NMR

Prion-like conversion during amyloid formation at atomic resolution

Released:
DOI: 10.2210/pdb2xku/pdb
PDB entry 2xku coloured by chain, ensemble of 30 models, front view.
PDB entry 2xku coloured by chain, ensemble of 30 models, side view.
PDB entry 2xku coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
Conformational conversion during amyloid formation at atomic resolution.
Eichner T, Kalverda AP, Thompson GS, Homans SW, Radford SE
Mol Cell 41 161-72 (2011)
PMID: 21255727

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158314 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-2-microglobulin Chain: A
Molecule details ›
Chain: A
Length: 94 amino acids
Theoretical weight: 11.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61769 (Residues: 27-119; Coverage: 94%)
Gene names: B2M, CDABP0092, HDCMA22P
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 91%
Refinement method: NONE
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

Molecular chaperones in protein folding and proteostasis.
Hartl et al. (2011)
17 more

16 mentions without citation

Understanding the complex mechanisms of β2-microglobulin amyloid assembly.
Eichner et al. (2011)
15 more