Cellular and Molecular Life Sciences CMLS

, Volume 62, Issue 24, pp 2956–2973

Trefoil factors

Structure of mammalian trefoil factors and functional insights
Multi-author Review

DOI: 10.1007/s00018-005-5484-6

Cite this article as:
Thim, L. & May, F.E.B. Cell. Mol. Life Sci. (2005) 62: 2956. doi:10.1007/s00018-005-5484-6

Abstract.

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.

Key words.

Trefoil Factors TFF domain homodimer heterodimer spasmolytic polypeptide pS2, mucins Helicobacter pylori 

Copyright information

© Birkhäuser Verlag, Basel 2005

Authors and Affiliations

  1. 1.Protein EngineeringMåløvDenmark
  2. 2.Nothern Institute for Cancer Research, The Medical SchoolUniversity of NewcastleNewcastle Upon TyneUnited Kingdom