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1pe3

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Solution structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3)

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Retrieved from "http://52.214.119.220/wiki/index.php/1pe3"

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-[[Image:1pe3.gif|left|200px]]<br />
-<applet load="1pe3" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1pe3" />
-'''Solution structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3)'''<br />
-==Overview==
+==Solution structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3)==
-The trefoil protein TFF3 forms a homodimer (via a disulfide linkage) that, is thought to have increased biological activity over the monomer. The, solution structure of the TFF3 dimer has been determined by NMR and, compared with the structure of the TFF3 monomer and with other trefoil, dimer structures (TFF1 and TFF2). The most significant structural, differences between the trefoil domain in the monomer and dimer TFF3 are, in the orientations of the N-terminal 3(10)-helix (residues 10-12) and in, the presence in the dimer of an additional 3(10)-helix (residues 53-55), outside of the core region. The TFF3 dimer forms a more compact structure, as compared with the TFF1 dimer where the two trefoil domains are, connected by a flexible region with the monomer units being at variable, distances from each other and in many different orientations. Although, TFF2 is also a compact structure, the dispositions of its monomer units, are very different from those of TFF3. The structural differences between, the dimers result in the two putative receptor/ligand binding sites that, remain solvent exposed in the dimeric structures having very different, dispositions in the different dimers. Such differences have significant, implications for the mechanism of action and functional specificity for, the TFF class of proteins.
+<StructureSection load='1pe3' size='340' side='right'caption='[[1pe3]]' scene=''>
+== Structural highlights ==
-==Disease==
+<table><tr><td colspan='2'>[[1pe3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PE3 FirstGlance]. <br>
-Known disease associated with this structure: Pitt-Hopkins syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602272 602272]]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1pe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pe3 OCA], [https://pdbe.org/1pe3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pe3 RCSB], [https://www.ebi.ac.uk/pdbsum/1pe3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pe3 ProSAT]</span></td></tr>
-==About this Structure==
+</table>
-PE3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PE3 OCA].
+== Function ==
+[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>
-==Reference==
+== Evolutionary Conservation ==
-Solution structure of the disulfide-linked dimer of human intestinal trefoil factor (TFF3): the intermolecular orientation and interactions are markedly different from those of other dimeric trefoil proteins., Muskett FW, May FE, Westley BR, Feeney J, Biochemistry. 2003 Dec 30;42(51):15139-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14690424 14690424]
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/1pe3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pe3 ConSurf].
+<div style="clear:both"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Feeney, J.]]
+[[Category: Feeney J]]
-[[Category: May, F.E.]]
+[[Category: May FE]]
-[[Category: Muskett, F.W.]]
+[[Category: Muskett FW]]
-[[Category: Westley, B.R.]]
+[[Category: Westley BR]]
-[[Category: intestinal trefoil factor]]
-[[Category: itf]]
-[[Category: nmr spectroscopy]]
-[[Category: solution structure]]
-[[Category: tff3]]
-[[Category: tff3 dimer]]
-[[Category: trefoil factor family]]
-[[Category: trefoil motif]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:42:40 2007''

1pe3

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Current revision

Solution structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3)

Structural highlights

Function

Evolutionary Conservation

References

Contents

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