2OOP

Structure of Tyr7-PYY in solution

2OOP の概要

• エントリーDOI: 10.2210/pdb2oop/pdb
• 関連するPDBエントリー: 1RUU 2OON 2OOO
• 分子名称: Peptide YY (1 entity in total)
• 機能のキーワード: helical haripin, folding, hormone
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P68005
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4337.79

構造登録者

Zerbe, O.,Neumoin, A.,Mares, J. (登録日: 2007-01-26, 公開日: 2007-12-25, 最終更新日: 2024-11-20)

主引用文献

Neumoin, A.,Mares, J.,Lerch-Bader, M.,Bader, R.,Zerbe, O.
Probing the formation of stable tertiary structure in a model miniprotein at atomic resolution: determinants of stability of a helical hairpin.
J.Am.Chem.Soc., 129:8811-8817, 2007

PubMed Abstract: The minimal model system to study the basic principles of protein folding is the hairpin. The formation of beta-hairpins, which are the basic components of antiparallel beta-sheets, has been studied extensively in the past decade, but much less is known about helical hairpins. Here, we probe hairpin formation between a polyproline type-II helix and an alpha-helix as present in the natural miniprotein peptide YY (PYY). Both turn sequence and interactions of aromatic side chains from the C-terminal alpha-helix with the pockets formed by N-terminal Pro residues are shown by site-directed mutagenesis and solution NMR spectroscopy in different solvent systems to be important determinants of backbone dynamics and hairpin stability, suggesting a close analogy with some beta-hairpin structures. It is shown that multiple relatively weak contacts between the helices are necessary for the formation of the helical hairpin studied here, whereas the type-I beta-turn acts like a hinge, which through certain single amino acid substitutions is destabilized such that hairpin formation is completely abolished. Denaturation and renaturation of tertiary structure by temperature or cosolvents were probed by measuring changes of chemical shifts. Folding of PYY is both reversible and cooperative as inferred from the sigmoidal denaturation curves displayed by residues at the interface of the helical hairpin. Such miniproteins thus feature an important hallmark of globular proteins and should provide a convenient system to study basic aspects of helical hairpin folding that are complementary to those derived from studies of beta-hairpins.

PubMed: 17580866
DOI: 10.1021/ja0716960

実験手法

SOLUTION NMR