2DEZ

Structure of human PYY

2DEZ の概要

• エントリーDOI: 10.2210/pdb2dez/pdb
• 関連するPDBエントリー: 2DF0
• NMR情報: BMRB: 7006
• 分子名称: Peptide YY (1 entity in total)
• 機能のキーワード: pp-fold, helix, neuropeptide
• 細胞内の位置: Secreted: P10082
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4314.80

構造登録者

Nygaard, R. (登録日: 2006-02-20, 公開日: 2006-07-18, 最終更新日: 2024-11-20)

主引用文献

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

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: 16819834
DOI: 10.1021/bi060359l

実験手法

SOLUTION NMR