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2dez
From Proteopedia
(New page: 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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'''Structure of human PYY'''<br /> | '''Structure of human PYY'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 2DEZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DEZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: pp-fold]] | [[Category: pp-fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:19:23 2008'' |
Revision as of 15:19, 15 February 2008
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Structure of human PYY
Overview
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
2DEZ is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Fri Feb 15 17:19:23 2008
Categories: Single protein | Nygaard, R. | NH2 | Helix | Neuropeptide | Peptide | Pp-fold
