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Structure of mammalian trefoil factors and functional insights

Lookup NU author(s): Dr Felicity May


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The present review will include the mammalian trefoil factors, TFF1, TFF2 and TFF3. It will summarise the amino acid sequences from different species, their posttranslational modifications and their structures determined by X-ray analysis and nuclear magnetic resonance studies. Trefoil factors all have a well-defined, structurally conserved trefoil domain. The trefoil domain consists of 42 or 43 amino acid residues and contains 6 cysteine residues that form disulphide bonds in a 1-5, 2-4 and 3-6 configuration. By the establishment of an additional intra-molecular disulphide bond at the C-terminal end, TFF1 and TFF3 form homodimers or heterodimers. This dimer formation of TFF1 and TFF3 will be discussed, and the possible implications for biological activity will be reviewed. The physicochemical characteristics including protease stability of trefoil factors will be summarised. The biological implications of different molecular forms of trefoil factors and their interaction with mucins will be discussed together with other functional insights. © Birkhäuser Verlag, 2005.

Publication metadata

Author(s): Thim L, May FEB

Publication type: Review

Publication status: Published

Journal: Cellular and Molecular Life Sciences

Year: 2005

Volume: 62

Issue: 24

Pages: 2956-2973

Print publication date: 01/12/2005

ISSN (print): 1420-682X

ISSN (electronic): 1420-9071


DOI: 10.1007/s00018-005-5484-6

PubMed id: 16374584