2DEZ
Structure of human PYY
Summary for 2DEZ
| Entry DOI | 10.2210/pdb2dez/pdb |
| Related | 2DF0 |
| NMR Information | BMRB: 7006 |
| Descriptor | Peptide YY (1 entity in total) |
| Functional Keywords | pp-fold, helix, neuropeptide |
| Cellular location | Secreted: P10082 |
| Total number of polymer chains | 1 |
| Total formula weight | 4314.80 |
| Authors | Nygaard, R. (deposition date: 2006-02-20, release date: 2006-07-18, Last modification date: 2024-11-20) |
| Primary citation | Nygaard, R.,Nielbo, S.,Schwartz, T.W.,Poulsen, F.M. The PP-Fold Solution Structure of Human Polypeptide YY and Human PYY3-36 As Determined by NMR(,) Biochemistry, 45:8350-8357, 2006 Cited by PubMed Abstract: 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. PubMed: 16819834DOI: 10.1021/bi060359l PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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