The solution structure of the disulphide-linked homodimer of the human trefoil protein TFF1

被引：41
作者：
Williams, MA
Westley, BR
May, FEB
Feeney, J
机构：
[1] Natl Inst Med Res, Mol Struct Div, London NW7 1AA, England
[2] Newcastle Univ, Royal Victoria Infirm, Dept Pathol, Newcastle Upon Tyne NE1 4LP, Tyne & Wear, England
[3] UCL, Dept Biochem & Mol Biol, London WC1E 6BT, England
来源：
FEBS LETTERS | 2001年 / 493卷 / 2-3期
基金：
英国医学研究理事会;
关键词：
trefoil factor family; TFF1; dimer; nuclear magnetic resonance; solution structure;
D O I：
10.1016/S0014-5793(01)02276-1
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 non investigate the structure of the homodimer formed bg 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. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. AU rights reserved.
引用
收藏
页码：70 / 74
页数：5
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