Thim L, May F E B
Protein Engineering, Novo Nordisk A/S, 2760 Måløv, Denmark.
Cell Mol Life Sci. 2005 Dec;62(24):2956-73. doi: 10.1007/s00018-005-5484-6.
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.
本综述将涵盖哺乳动物三叶因子TFF1、TFF2和TFF3。它将总结来自不同物种的氨基酸序列、它们的翻译后修饰以及通过X射线分析和核磁共振研究确定的结构。三叶因子都具有明确的、结构保守的三叶结构域。三叶结构域由42或43个氨基酸残基组成，包含6个半胱氨酸残基，它们以1-5、2-4和3-6的构型形成二硫键。通过在C末端建立一个额外的分子内二硫键，TFF1和TFF3形成同二聚体或异二聚体。将讨论TFF1和TFF3的这种二聚体形成，并综述其对生物活性的可能影响。将总结三叶因子的物理化学特性，包括蛋白酶稳定性。将讨论三叶因子不同分子形式的生物学意义及其与黏蛋白的相互作用以及其他功能见解。
