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New page: left|200px<br /> <applet load="2dez" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dez" /> '''Structure of human PYY'''<br /> ==Overview...
 
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[[Image:2dez.gif|left|200px]]<br />
<applet load="2dez" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2dez" />
'''Structure of human PYY'''<br />


==Overview==
==Structure of human PYY==
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.
<StructureSection load='2dez' size='340' side='right'caption='[[2dez]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2dez]] 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=2DEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DEZ FirstGlance]. <br>
</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>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dez OCA], [https://pdbe.org/2dez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dez RCSB], [https://www.ebi.ac.uk/pdbsum/2dez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dez ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[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/de/2dez_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2dez ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==About this Structure==
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>
2DEZ 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=2DEZ OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 2dez" style="background-color:#fffaf0;"></div>
[[Category: Nygaard, R.]]
== References ==
[[Category: NH2]]
<references/>
[[Category: helix]]
__TOC__
[[Category: neuropeptide]]
</StructureSection>
[[Category: peptide]]
[[Category: Homo sapiens]]
[[Category: pp-fold]]
[[Category: Large Structures]]
 
[[Category: Nygaard R]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:31:38 2007''

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Structure of human PYY

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