2df0

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(New page: 200px<br /> <applet load="2df0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2df0" /> '''Solution structure of human PYY3-36'''<br /...)
Current revision (00:52, 21 November 2024) (edit) (undo)
 
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[[Image:2df0.gif|left|200px]]<br />
 
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<applet load="2df0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2df0" />
 
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'''Solution structure of human PYY3-36'''<br />
 
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==Overview==
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==Solution structure of human PYY3-36==
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PYY3-36 is a biopharmaceutical antiobesity agent under development as well, as an endogenous satiety hormone, which is generated by dipeptidyl, peptidase-IV digestion of polypetide YY (PYY), and in contrast to the, parent hormone, PYY is highly selective for the Y2 versus the Y1 receptor., NMR analysis revealed a highly ordered, back-folded structure for human, PYY in aqueous solution similar to the classical PP-fold structure of, pancreatic polypeptide. The NMR analysis of PYY3-36 also showed a folded, structure resembling a PP-fold, which however was characterized by far, fewer long distance NOEs than the PP-fold observed in the full-length, peptide. This suggests that either a conformational change has occurred in, the N-terminal segment of PYY3-36 or that this segments is characterized, by larger dynamics. The study supports the notion that the PP-fold is, crucial for establishing simultaneous interactions with two subsites in, the receptor for binding of, respectively, the N- and C-terminal ends of, PYY. The Y2 receptor only requires recognition of the C-terminal segment, of the molecule as displayed by the Y2 selective PYY3-36.
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<StructureSection load='2df0' size='340' side='right'caption='[[2df0]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2df0]] is a 1 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=2DF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DF0 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2df0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2df0 OCA], [https://pdbe.org/2df0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2df0 RCSB], [https://www.ebi.ac.uk/pdbsum/2df0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2df0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PYY_HUMAN PYY_HUMAN] This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/df/2df0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2df0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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PYY3-36 is a biopharmaceutical antiobesity agent under development as well as an endogenous satiety hormone, which is generated by dipeptidyl peptidase-IV digestion of polypetide YY (PYY), and in contrast to the parent hormone, PYY is highly selective for the Y2 versus the Y1 receptor. NMR analysis revealed a highly ordered, back-folded structure for human PYY in aqueous solution similar to the classical PP-fold structure of pancreatic polypeptide. The NMR analysis of PYY3-36 also showed a folded structure resembling a PP-fold, which however was characterized by far fewer long distance NOEs than the PP-fold observed in the full-length peptide. This suggests that either a conformational change has occurred in the N-terminal segment of PYY3-36 or that this segments is characterized by larger dynamics. The study supports the notion that the PP-fold is crucial for establishing simultaneous interactions with two subsites in the receptor for binding of, respectively, the N- and C-terminal ends of PYY. The Y2 receptor only requires recognition of the C-terminal segment of the molecule as displayed by the Y2 selective PYY3-36.
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==About this Structure==
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The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR.,Nygaard R, Nielbo S, Schwartz TW, Poulsen FM Biochemistry. 2006 Jul 11;45(27):8350-7. PMID:16819834<ref>PMID:16819834</ref>
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2DF0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DF0 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR., Nygaard R, Nielbo S, Schwartz TW, Poulsen FM, Biochemistry. 2006 Jul 11;45(27):8350-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16819834 16819834]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 2df0" style="background-color:#fffaf0;"></div>
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[[Category: Nygaard, R.]]
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== References ==
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[[Category: NH2]]
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<references/>
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[[Category: amphipathic]]
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__TOC__
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[[Category: helix]]
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</StructureSection>
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[[Category: neuropeptide]]
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[[Category: Homo sapiens]]
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[[Category: peptide]]
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[[Category: Large Structures]]
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[[Category: pp-fold]]
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[[Category: Nygaard R]]
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[[Category: pyy]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:31:40 2007''
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Current revision

Solution structure of human PYY3-36

PDB ID 2df0

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