6IMG

Solution Structure of Bicyclic Peptide pb-13

6IMG の概要

• エントリーDOI: 10.2210/pdb6img/pdb
• 分子名称: (ACE)-GLY-CYS-PRO-CYS-ILE-TRP-PRO-GLU-LEU-CYS-PRO-TRP-ILE-ARG-SER-CYS-(NH2) (1 entity in total)
• 機能のキーワード: bicyclic peptide, cystine bridge, proline rich, de novo protein
• 由来する生物種: Enterobacteria phage M13
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1888.31

構造登録者

Yao, H.,Lin, P.,Zha, J.,Zha, M.,Zhao, Y.,Wu, C. (登録日: 2018-10-22, 公開日: 2019-08-28, 最終更新日: 2024-11-13)

主引用文献

Lin, P.,Yao, H.,Zha, J.,Zhao, Y.,Wu, C.
Ordered and Isomerically Stable Bicyclic Peptide Scaffolds Constrained through Cystine Bridges and Proline Turns.
Chembiochem, 20:1514-1518, 2019

PubMed Abstract: Bicyclic peptides are attractive scaffolds for the design of potent protein binders and new therapeutics. However, peptide bicycles constrained through disulfide bonds are rarely stable or tolerant to sequence manipulation owing to disulfide isomerization, especially for peptides lacking a regular secondary structure. Herein, we report the discovery and identification of a class of bicyclic peptide scaffolds with ordered but irregular secondary structures. These peptides have a conserved cysteine/proline framework for directing the oxidative folding into a fused bicyclic structure that consists of four irregular turns and a 3 helix (characterized by NMR spectroscopy). This work shows that bicyclic peptides can be stabilized into ordered structures by manipulating both the disulfide bonds and proline-stabilized turns. In turn, this could inspire the design and engineering of multicyclic peptides with new structures and benefit the development of novel protein binders and therapeutics.

PubMed: 30770638
DOI: 10.1002/cbic.201800788

実験手法

SOLUTION NMR