Browse by author
Lookup NU author(s): Dr Felicity May
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
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
URL: http://dx.doi.org/10.1007/s00018-005-5484-6
DOI: 10.1007/s00018-005-5484-6
PubMed id: 16374584
