The solution structure of the disulphide-linked homodimer of the human trefoil protein TFF1

The trefoil factor family protein, TFF1, forms a homodimer, via a disulphide linkage, that has greater activity in wound healing assays than the monomer. Having previously determined a high-resolution solution structure of a monomeric analogue of TFF1, we now investigate the structure of the homodim...

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Bibliographic Details
Published in:FEBS letters 2001-03, Vol.493 (2), p.70-74
Main Authors: Williams, Mark A., Westley, Bruce R., May, Felicity E.B., Feeney, James
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Calcium - pharmacology
Cysteine - chemistry
Dimerization
Disulfides - chemistry
Growth Substances - chemistry
HSQC, heteronuclear single quantum correlation spectroscopy
Humans
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Mucins
Muscle Proteins
Neuropeptides
NMR, nuclear magnetic resonance
NOE, nuclear Overhauser enhancement
NOESY, nuclear Overhauser enhancement spectroscopy
Nuclear magnetic resonance
Osmolar Concentration
Peptides - chemistry
Protein Conformation
Protein Structure, Quaternary
Proteins - chemistry
Proteins - genetics
Solution structure
Solutions
TFF1
TFF1 dimer
Trefoil factor family
Trefoil Factor-1
Trefoil Factor-2
Trefoil Factor-3
Tumor Suppressor Proteins
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Summary:The trefoil factor family protein, TFF1, forms a homodimer, via a disulphide linkage, that has greater activity in wound healing assays than the monomer. Having previously determined a high-resolution solution structure of a monomeric analogue of TFF1, we now investigate the structure of the homodimer formed by the native sequence. The two putative receptor/ligand recognition domains are found to be well separated, at opposite ends of a flexible linker. This contrasts sharply with the known fixed and compact arrangement of the two trefoil domains of the closely related TFF2, and has significant implications for the mechanism of action and functional specificity of the TFF of proteins.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(01)02276-1