› 1py4

X-ray diffraction
2.9Å resolution

Beta2 microglobulin mutant H31Y displays hints for amyloid formations

Released:
DOI: 10.2210/pdb1py4/pdb
PDB entry 1py4 coloured by chain, front view.
PDB entry 1py4 coloured by chain, side view.
PDB entry 1py4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
beta2-microglobulin H31Y variant 3D structure highlights the protein natural propensity towards intermolecular aggregation.
Rosano C, Zuccotti S, Mangione P, Giorgetti S, Bellotti V, Pettirossi F, Corazza A, Viglino P, Esposito G, Bolognesi M
J Mol Biol 335 1051-64 (2004)
PMID: 14698299

Function and Biology Details

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

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 100 amino acids
Theoretical weight: 11.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61769 (Residues: 21-119; Coverage: 100%)
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
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: C2221
Unit cell:
a: 105.195Å b: 150.166Å c: 93.671Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.241 0.24 0.313
Expression system: Escherichia coli

Quick links

Citations

2 review citations

beta(2)-microglobulin: from physiology to amyloidosis.
Heegaard NH. (2009)
1 more

3 mentions without citation

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