2df0
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2df0.gif|left|200px]] | [[Image:2df0.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2df0", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | | | + | or leave the SCENE parameter empty for the default display. |
- | | | + | --> |
- | + | {{STRUCTURE_2df0| PDB=2df0 | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''Solution structure of human PYY3-36''' | '''Solution structure of human PYY3-36''' | ||
Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 2DF0 is a [[Single protein]] structure | + | 2DF0 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DF0 OCA]. |
==Reference== | ==Reference== | ||
Line 25: | Line 22: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Nygaard, R.]] | [[Category: Nygaard, R.]] | ||
- | [[Category: | + | [[Category: Amphipathic]] |
- | [[Category: | + | [[Category: Helix]] |
- | [[Category: | + | [[Category: Neuropeptide]] |
- | [[Category: | + | [[Category: Peptide]] |
- | [[Category: | + | [[Category: Pp-fold]] |
- | [[Category: | + | [[Category: Pyy]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:18:10 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 21:18, 3 May 2008
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. 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 Sun May 4 00:18:10 2008
Categories: Single protein | Nygaard, R. | Amphipathic | Helix | Neuropeptide | Peptide | Pp-fold | Pyy