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Lookup NU author(s): Professor Bruce Westley,
Dr Felicity May
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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.
Author(s): Williams M, Westley B, May F, Feeney J
Publication type: Article
Publication status: Published
Journal: FEBS Letters
Print publication date: 30/03/2001
ISSN (print): 0014-5793
ISSN (electronic): 1873-3468
PubMed id: 11286998
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