Structural highlights
Function
[TFF1_HUMAN] Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. May inhibit the growth of calcium oxalate crystals in urine.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The solution structure of the disulphide-linked homodimer of the human trefoil protein TFF1.,Williams MA, Westley BR, May FE, Feeney J FEBS Lett. 2001 Mar 30;493(2-3):70-4. PMID:11286998[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chutipongtanate S, Nakagawa Y, Sritippayawan S, Pittayamateekul J, Parichatikanond P, Westley BR, May FE, Malasit P, Thongboonkerd V. Identification of human urinary trefoil factor 1 as a novel calcium oxalate crystal growth inhibitor. J Clin Invest. 2005 Dec;115(12):3613-22. Epub 2005 Nov 23. PMID:16308573 doi:http://dx.doi.org/10.1172/JCI25342
- ↑ Williams MA, Westley BR, May FE, Feeney J. The solution structure of the disulphide-linked homodimer of the human trefoil protein TFF1. FEBS Lett. 2001 Mar 30;493(2-3):70-4. PMID:11286998
