@article{0c292c9070ec11dcbee902004c4f4f50,
title = "The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR",
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.",
author = "Rie Nygaard and Steen Nielbo and Schwartz, {Thue W} and Poulsen, {Flemming M}",
note = "Keywords: Amino Acid Sequence; Animals; COS Cells; Cercopithecus aethiops; Humans; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Peptide YY; Protein Conformation; Protein Folding; Receptors, Gastrointestinal Hormone; Solutions; Transfection",
year = "2006",
doi = "10.1021/bi060359l",
language = "English",
volume = "45",
pages = "8350--7",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "27",
}