› 3g7v

X-ray diffraction
1.86Å resolution

Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein

Released:
DOI: 10.2210/pdb3g7v/pdb
PDB entry 3g7v coloured by chain, front view.
PDB entry 3g7v coloured by chain, side view.
PDB entry 3g7v coloured by chain, top view.
Source organisms:
Primary publication:
Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process.
Wiltzius JJ, Sievers SA, Sawaya MR, Eisenberg D
Protein Sci 18 1521-30 (2009)
PMID: 19475663

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142517 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Islet amyloid polypeptide; Maltose/maltodextrin-binding periplasmic protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 408 amino acids
Theoretical weight: 44.44 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-392; Coverage: 99%)
  • Canonical: P10997 (Residues: 34-70; Coverage: 55%)
Gene names: IAPP, JW3994, b4034, malE
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand SO4 15 x SO4
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 104.025Å b: 96.407Å c: 103.996Å
α: 90° β: 90.53° γ: 90°
R-values:
R R work R free
0.178 0.176 0.205
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Islet amyloid polypeptide, islet amyloid, and diabetes mellitus.
Westermark et al. (2011)
19 more

5 mentions without citation

Misfolded proteins in Alzheimer's disease and type II diabetes.
DeToma et al. (2012)
4 more