› 2l86

Solution NMR

Solution NMR structure of human amylin in SDS micelles at pH 7.3

Released:
DOI: 10.2210/pdb2l86/pdb
PDB entry 2l86 coloured by chain, ensemble of 20 models, front view.
PDB entry 2l86 coloured by chain, ensemble of 20 models, side view.
PDB entry 2l86 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment.
Nanga RP, Brender JR, Vivekanandan S, Ramamoorthy A
Biochim Biophys Acta 1808 2337-42 (2011)
PMID: 21723249

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Islet amyloid polypeptide Chain: A
Molecule details ›
Chain: A
Length: 38 amino acids
Theoretical weight: 3.91 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P10997 (Residues: 34-70; Coverage: 55%)
Gene name: IAPP
Sequence domains: Calcitonin / CGRP / IAPP family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 51%
Refinement method: torsion angle dynamics, simulated annealing
Expression system: Not provided

Quick links

Citations

18 review citations

Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
Cao et al. (2013)
17 more

52 mentions without citation

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.
Nguyen et al. (2021)
51 more