› 4qxx

X-ray diffraction
1.44Å resolution

Structure of the amyloid forming peptide GNLVS (residues 26-30) from the eosinophil major basic protein (EMBP)

Released:
DOI: 10.2210/pdb4qxx/pdb
PDB entry 4qxx coloured by chain, front view.
PDB entry 4qxx coloured by chain, side view.
PDB entry 4qxx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Toxicity of eosinophil MBP is repressed by intracellular crystallization and promoted by extracellular aggregation.
Soragni A, Yousefi S, Stoeckle C, Soriaga AB, Sawaya MR, Kozlowski E, Schmid I, Radonjic-Hoesli S, Boutet S, Williams GJ, Messerschmidt M, Seibert MM, Cascio D, Zatsepin NA, Burghammer M, Riekel C, Colletier JP, Riek R, Eisenberg DS, Simon HU
Mol Cell 57 1011-1021 (2015)
PMID: 25728769

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146737 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Eosinophil granule major basic protein Chain: Z
Molecule details ›
Chain: Z
Length: 5 amino acids
Theoretical weight: 489 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P13727 (Residues: 131-135; Coverage: 2%)
Gene names: MBP, PRG2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Unit cell:
a: 4.755Å b: 16.816Å c: 35.759Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.164 0.192
Expression system: Not provided

Quick links

Citations

23 review citations

Cellular and molecular immunologic mechanisms in patients with atopic dermatitis.
Werfel et al. (2016)
22 more

2 mentions without citation

Toxicity of eosinophil MBP is repressed by intracellular crystallization and promoted by extracellular aggregation.
Soragni et al. (2015)
1 more