The solution structure of the disulphide-linked homodimer of the human trefoil protein TFF1
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- 作者：Williams ; Mark A. ; Westley ; Bruce R. ; May ; Felicity E.B. ; Feeney ; James
- 关键词：Trefoil factor family ; TFF1 ; TFF1 dimer ; Nuclear magnetic resonance ; Solution structure ; HSQC ; heteronuclear single quantum correlation spectroscopy ; NMR ; nuclear magnetic resonance ; NOE ; nuclear Overhauser enhancement ; NOESY ; nuclear Overhauser enhanceme
- 刊名：FEBS Letters
- 出版年：2001
- 出版时间：March 30, 2001
- 年：2001
- 卷：493
- 期：2-3
- 页码：70-74
- 全文大小：150 K
文摘
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.