› 2poa

Solution NMR

Schistosoma mansoni Sm14 Fatty Acid-Binding Protein: improvement of protein stability by substitution of the single Cys62 residue

Released:
DOI: 10.2210/pdb2poa/pdb
PDB entry 2poa coloured by chain, ensemble of 17 models, front view.
PDB entry 2poa coloured by chain, ensemble of 17 models, side view.
PDB entry 2poa coloured by chain, ensemble of 17 models, top view.
Source organism: Schistosoma mansoni
Primary publication:
Stability improvement of the fatty acid binding protein Sm14 from S. mansoni by Cys replacement: structural and functional characterization of a vaccine candidate.
Ramos CR, Spisni A, Oyama S, Sforça ML, Ramos HR, Vilar MM, Alves AC, Figueredo RC, Tendler M, Zanchin NI, Pertinhez TA, Ho PL
Biochim Biophys Acta 1794 655-62 (2009)
PMID: 19150418

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-151526 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
14 kDa fatty acid-binding protein Chain: A
Molecule details ›
Chain: A
Length: 133 amino acids
Theoretical weight: 14.86 KDa
Source organism: Schistosoma mansoni
Expression system: Escherichia coli
UniProt:
  • Canonical: P29498 (Residues: 1-133; Coverage: 100%)
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 86%
Refinement method: torsion angle dynamics using dyana software and further minimization with discover module of the insight package
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Developing vaccines to combat hookworm infection and intestinal schistosomiasis.
Hotez et al. (2010)
7 more

1 mention without citation

Valproic acid protects against haemorrhagic shock-induced signalling changes via PPARγ activation in an in vitro model.
Zuckermann et al. (2015)