2df0

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of human PYY3-36

Structural highlights

2df0 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PYY_HUMAN This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility.

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

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nygaard R, Nielbo S, Schwartz TW, Poulsen FM. The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR. Biochemistry. 2006 Jul 11;45(27):8350-7. PMID:16819834 doi:10.1021/bi060359l

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2df0"

Categories: Homo sapiens | Large Structures | Nygaard R

@@ Line 1: / Line 1: @@
 ==Solution structure of human PYY3-36==
-<StructureSection load='2df0' size='340' side='right'caption='[[2df0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2df0' size='340' side='right'caption='[[2df0]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2df0]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DF0 FirstGlance]. <br>
+<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>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dez|2dez]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2df0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2df0 OCA], [http://pdbe.org/2df0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2df0 RCSB], [http://www.ebi.ac.uk/pdbsum/2df0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2df0 ProSAT]</span></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=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>
 </table>
 == Function ==
-[[http://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.
+[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]]
@@ Line 15: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/df/2df0_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Nygaard, R]]
+[[Category: Nygaard R]]
-[[Category: Amphipathic]]
-[[Category: Helix]]
-[[Category: Neuropeptide]]
-[[Category: Pp-fold]]
-[[Category: Pyy]]

2df0

From Proteopedia

Current revision

Solution structure of human PYY3-36

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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