› 1pe3

Solution NMR

Solution structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3)

Released:
DOI: 10.2210/pdb1pe3/pdb
PDB entry 1pe3 coloured by chain, ensemble of 47 models, front view.
PDB entry 1pe3 coloured by chain, ensemble of 47 models, side view.
PDB entry 1pe3 coloured by chain, ensemble of 47 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the disulfide-linked dimer of human intestinal trefoil factor (TFF3): the intermolecular orientation and interactions are markedly different from those of other dimeric trefoil proteins.
Muskett FW, May FE, Westley BR, Feeney J
Biochemistry 42 15139-47 (2003)
PMID: 14690424

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170489 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trefoil factor 3 Chains: 1, 2
Molecule details ›
Chains: 1, 2
Length: 59 amino acids
Theoretical weight: 6.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q07654 (Residues: 22-80; Coverage: 100%)
Gene names: ITF, TFF3, TFI
Sequence domains: Trefoil (P-type) domain
Structure domains: Spasmolytic Protein, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Expression profiles of MUC mucins and trefoil factor family (TFF) peptides in the intrahepatic biliary system: physiological distribution and pathological significance.
Sasaki et al. (2007)
6 more

4 mentions without citation

Structure, Function, and Therapeutic Potential of the Trefoil Factor Family in the Gastrointestinal Tract.
Braga Emidio et al. (2020)
3 more