2df0
From Proteopedia
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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] with NH2 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 Mon Nov 12 21:31:40 2007
Categories: Single protein | Nygaard, R. | NH2 | Amphipathic | Helix | Neuropeptide | Peptide | Pp-fold | Pyy
