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

Lookup NU author(s): Professor Bruce Westley, Dr Felicity May

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Abstract

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. © 2001 Federation of European Biochemical Societies.

Publication metadata

Author(s): Williams M, Westley B, May F, Feeney J

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 2001

Volume: 493

Issue: 2-3

Pages: 70-74

Print publication date: 30/03/2001

ISSN (print): 0014-5793

ISSN (electronic): 1873-3468

URL: http://dx.doi.org/10.1016/S0014-5793(01)02276-1

DOI: 10.1016/S0014-5793(01)02276-1

PubMed id: 11286998

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