7NPQ

Crystal structure of the human LL37(17-29) I24C mutant antimicrobial peptide

7NPQ の概要

• エントリーDOI: 10.2210/pdb7npq/pdb
• 分子名称: Cathelicidin antimicrobial peptide (2 entities in total)
• 機能のキーワード: ll-37, functional fibril, helical fibril, amps, cys mutant, design, antimicrobial peptide, antimicrobial protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 3428.22

構造登録者

Landau, M.,Engelberg, Y. (登録日: 2021-02-28, 公開日: 2022-02-16, 最終更新日: 2024-11-06)

主引用文献

Engelberg, Y.,Ragonis-Bachar, P.,Landau, M.
Rare by Natural Selection: Disulfide-Bonded Supramolecular Antimicrobial Peptides.
Biomacromolecules, 23:926-936, 2022

PubMed Abstract: Human LL-37 is an antimicrobial peptide forming thermostable supramolecular fibrils that surround bacterial cells. The crystal structure of LL-37 bearing an I24C substitution of most buried position in the fibril revealed disulfide-bonded dimers that further assembled into a fibrillar structure of densely packed helices We further demonstrated the position-dependent controllable antibacterial activity of LL-37 I24C and other cysteine mutants, mediated by regulation of intermolecular disulfide bonds and their role in the formation of supramolecular structures. The morphology of the fibrils and their antibacterial mechanism of action might be dependent on their interactions with specific bacteria. The significant effect of disulfide bonds on the assembly into supramolecular structures and their sensitivity to reducing/oxidizing conditions may explain why short helical antimicrobial peptides with a single cysteine and an odd number of cysteines are selected against in nature.

PubMed: 35061360
DOI: 10.1021/acs.biomac.1c01353

実験手法

X-RAY DIFFRACTION (1.5 Å)