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

MA Williams, BR Westley, FEB May, J Feeney - FEBS letters, 2001 - Wiley Online Library
MA Williams, BR Westley, FEB May, J Feeney
FEBS letters, 2001Wiley Online Library
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 …
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.
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