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| | <StructureSection load='6v1c' size='340' side='right'caption='[[6v1c]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='6v1c' size='340' side='right'caption='[[6v1c]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6v1c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V1C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V1C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6v1c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V1C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4A4:N/A4-O-[2-(ACETYLAMINO)-2-DEOXY-ALPHA-D-GLUCOPYRANOSYL]-BETA-D-GALACTOPYRANOSE'>4A4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TFF3, ITF, TFI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6v1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v1c OCA], [https://pdbe.org/6v1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v1c RCSB], [https://www.ebi.ac.uk/pdbsum/6v1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v1c ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6v1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v1c OCA], [http://pdbe.org/6v1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v1c RCSB], [http://www.ebi.ac.uk/pdbsum/6v1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v1c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TFF3_HUMAN TFF3_HUMAN]] Involved in the maintenance and repair of the intestinal mucosa. Promotes the mobility of epithelial cells in healing processes (motogen).<ref>PMID:11694446</ref> | + | [https://www.uniprot.org/uniprot/TFF3_HUMAN TFF3_HUMAN] Involved in the maintenance and repair of the intestinal mucosa. Promotes the mobility of epithelial cells in healing processes (motogen).<ref>PMID:11694446</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Goddard-Borger, E D]] | + | [[Category: Goddard-Borger ED]] |
| - | [[Category: Jarva, M A]] | + | [[Category: Jarva MA]] |
| - | [[Category: John, A]] | + | [[Category: John A]] |
| - | [[Category: Lingford, J P]] | + | [[Category: Lingford JP]] |
| - | [[Category: Scott, N E]] | + | [[Category: Scott NE]] |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Mucin binding protein]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| - | [[Category: Trefoil factor]]
| + | |
| Structural highlights
Function
TFF3_HUMAN Involved in the maintenance and repair of the intestinal mucosa. Promotes the mobility of epithelial cells in healing processes (motogen).[1]
Publication Abstract from PubMed
The mucosal epithelium secretes a host of protective disulfide-rich peptides, including the trefoil factors (TFFs). The TFFs increase the viscoelasticity of the mucosa and promote cell migration, though the molecular mechanisms underlying these functions have remained poorly defined. Here, we demonstrate that all TFFs are divalent lectins that recognise the GlcNAc-alpha-1,4-Gal disaccharide, which terminates some mucin-like O-glycans. Degradation of this disaccharide by a glycoside hydrolase abrogates TFF binding to mucins. Structural, mutagenic and biophysical data provide insights into how the TFFs recognise this disaccharide and rationalise their ability to modulate the physical properties of mucus across different pH ranges. These data reveal that TFF activity is dependent on the glycosylation state of mucosal glycoproteins and alludes to a lectin function for trefoil domains in other human proteins.
Trefoil factors share a lectin activity that defines their role in mucus.,Jarva MA, Lingford JP, John A, Soler NM, Scott NE, Goddard-Borger ED Nat Commun. 2020 May 13;11(1):2265. doi: 10.1038/s41467-020-16223-7. PMID:32404934[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Oertel M, Graness A, Thim L, Buhling F, Kalbacher H, Hoffmann W. Trefoil factor family-peptides promote migration of human bronchial epithelial cells: synergistic effect with epidermal growth factor. Am J Respir Cell Mol Biol. 2001 Oct;25(4):418-24. PMID:11694446 doi:http://dx.doi.org/10.1165/ajrcmb.25.4.4429
- ↑ Jarva MA, Lingford JP, John A, Soler NM, Scott NE, Goddard-Borger ED. Trefoil factors share a lectin activity that defines their role in mucus. Nat Commun. 2020 May 13;11(1):2265. doi: 10.1038/s41467-020-16223-7. PMID:32404934 doi:http://dx.doi.org/10.1038/s41467-020-16223-7
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