› 1hi7

Solution NMR

NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN TFF1, 10 STRUCTURES

Released:
DOI: 10.2210/pdb1hi7/pdb
PDB entry 1hi7 coloured by chain, ensemble of 10 models, front view.
PDB entry 1hi7 coloured by chain, ensemble of 10 models, side view.
PDB entry 1hi7 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
The solution structure of the disulphide-linked homodimer of the human trefoil protein TFF1.
Williams MA, Westley BR, May FE, Feeney J
FEBS Lett 493 70-4 (2001)
PMID: 11286998

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-137454 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trefoil factor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 60 amino acids
Theoretical weight: 6.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli HB101
UniProt:
  • Canonical: P04155 (Residues: 25-84; Coverage: 100%)
Gene names: BCEI, PS2, TFF1
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: simulated annealing
Expression system: Escherichia coli HB101

Quick links

Citations

4 review citations

Trefoil Factor Peptides and Gastrointestinal Function.
Aihara et al. (2017)
3 more

6 mentions without citation

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