› 3dgj

X-ray diffraction
1.8Å resolution

NNFGAIL segment from Islet Amyloid Polypeptide (IAPP or amylin)

Released:
DOI: 10.2210/pdb3dgj/pdb
PDB entry 3dgj coloured by chain, front view.
PDB entry 3dgj coloured by chain, side view.
PDB entry 3dgj coloured by chain, top view.
Source organism: Synthetic construct
Primary publication:
Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin).
Wiltzius JJ, Sievers SA, Sawaya MR, Cascio D, Popov D, Riekel C, Eisenberg D
Protein Sci 17 1467-74 (2008)
PMID: 18556473

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163480 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NNFGAIL peptide Chain: A
Molecule details ›
Chain: A
Length: 7 amino acids
Theoretical weight: 748 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID13
Spacegroup: P212121
Unit cell:
a: 26.19Å b: 4.897Å c: 31.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.16 0.217
Expression system: Not provided

Quick links

Citations

44 review citations

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

12 mentions without citation

Linking hIAPP misfolding and aggregation with type 2 diabetes mellitus: a structural perspective.
Hassan et al. (2022)
11 more