2df0
From Proteopedia
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| - | [[Image:2df0.gif|left|200px]] | + | [[Image:2df0.gif|left|200px]] |
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| - | '''Solution structure of human PYY3-36''' | + | {{Structure |
| + | |PDB= 2df0 |SIZE=350|CAPTION= <scene name='initialview01'>2df0</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of human PYY3-36''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2DF0 is a [ | + | 2DF0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DF0 OCA]. |
==Reference== | ==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:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/16819834 16819834] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Nygaard, R.]] | [[Category: Nygaard, R.]] | ||
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[[Category: pyy]] | [[Category: pyy]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:26:27 2008'' |
Revision as of 14:26, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of human PYY3-36
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
2DF0 is a Single protein structure of sequence from [1]. 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 Thu Mar 20 16:26:27 2008
Categories: Single protein | Nygaard, R. | NH2 | Amphipathic | Helix | Neuropeptide | Peptide | Pp-fold | Pyy
