› 5e5v

X-ray diffraction
1.24Å resolution

Structure of amyloid forming peptide NFGAILS (residues 22-28) from Islet Amyloid Polypeptide

Released:
DOI: 10.2210/pdb5e5v/pdb
PDB entry 5e5v coloured by chain, front view.
PDB entry 5e5v coloured by chain, side view.
PDB entry 5e5v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets.
Soriaga AB, Sangwan S, Macdonald R, Sawaya MR, Eisenberg D
J Phys Chem B 120 5810-6 (2016)
PMID: 26629790

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165584 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NFGAILS (22-28) from islet amyloid polypeptide, synthesized Chains: A, B
Molecule details ›
Chains: A, B
Length: 7 amino acids
Theoretical weight: 721 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P1
Unit cell:
a: 8.661Å b: 11.594Å c: 21.552Å
α: 86.39° β: 82.21° γ: 76.35°
R-values:
R R work R free
0.176 0.173 0.206
Expression system: Not provided

Quick links

Citations

8 review citations

Structural Studies of Amyloid Proteins at the Molecular Level.
Eisenberg et al. (2017)
7 more

4 mentions without citation

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