7L55

Solution NMR structure of the cyclic plant protein PDP-23 in DPC micelles

7L55 の概要

• エントリーDOI: 10.2210/pdb7l55/pdb
• 関連するPDBエントリー: 7L51 7L53 7L54
• NMR情報: BMRB: 30830
• 分子名称: Cyclic plant protein PDP-23 (1 entity in total)
• 機能のキーワード: paws derived peptide, macrocycle, plant protein
• 由来する生物種: Zinnia elegans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3135.51

構造登録者

Payne, C.D.,Rosengren, K.J. (登録日: 2020-12-21, 公開日: 2021-01-20, 最終更新日: 2024-10-23)

主引用文献

Payne, C.D.,Franke, B.,Fisher, M.F.,Hajiaghaalipour, F.,McAleese, C.E.,Song, A.,Eliasson, C.,Zhang, J.,Jayasena, A.S.,Vadlamani, G.,Clark, R.J.,Minchin, R.F.,Mylne, J.S.,Rosengren, K.J.
A chameleonic macrocyclic peptide with drug delivery applications.
Chem Sci, 12:6670-6683, 2021

PubMed Abstract: Head-to-tail cyclized peptides are intriguing natural products with unusual properties. The PawS-Derived Peptides (PDPs) are ribosomally synthesized as part of precursors for seed storage albumins in species of the daisy family, and are post-translationally excised and cyclized during proteolytic processing. Here we report a PDP twice the typical size and with two disulfide bonds, identified from seeds of . In water, synthetic PDP-23 forms a unique dimeric structure in which two monomers containing two β-hairpins cross-clasp and enclose a hydrophobic core, creating a square prism. This dimer can be split by addition of micelles or organic solvent and in monomeric form PDP-23 adopts open or closed V-shapes, exposing different levels of hydrophobicity dependent on conditions. This chameleonic character is unusual for disulfide-rich peptides and engenders PDP-23 with potential for cell delivery and accessing novel targets. We demonstrate this by conjugating a rhodamine dye to PDP-23, creating a stable, cell-penetrating inhibitor of the P-glycoprotein drug efflux pump.

PubMed: 34040741
DOI: 10.1039/d1sc00692d

実験手法

SOLUTION NMR