› 5k5g

Solution NMR

Structure of human islet amyloid polypeptide in complex with an engineered binding protein

Released:
DOI: 10.2210/pdb5k5g/pdb
PDB entry 5k5g coloured by chain, ensemble of 10 models, front view.
PDB entry 5k5g coloured by chain, ensemble of 10 models, side view.
PDB entry 5k5g coloured by chain, ensemble of 10 models, top view.
Source organisms:
Primary publication:
β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor.
Mirecka EA, Feuerstein S, Gremer L, Schröder GF, Stoldt M, Willbold D, Hoyer W
Sci Rep 6 33474 (2016)
PMID: 27641459

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145615 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Islet amyloid polypeptide Chain: A
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 3.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P10997 (Residues: 34-70; Coverage: 55%)
Gene name: IAPP
Sequence domains: Calcitonin / CGRP / IAPP family
HI18 Chains: B, C
Molecule details ›
Chains: B, C
Length: 69 amino acids
Theoretical weight: 7.8 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
Structure domains: Immunoglobulin FC, subunit C

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 42%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Affibody Molecules in Biotechnological and Medical Applications.
Ståhl et al. (2017)
4 more

6 mentions without citation

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