6S6M

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

6S6M の概要

• エントリーDOI: 10.2210/pdb6s6m/pdb
• 分子名称: Cathelicidin antimicrobial peptide (2 entities in total)
• 機能のキーワード: helical and tubular fibril structure of a human derived antimicrobial peptide, protein fibril
• 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: 3448.25

構造登録者

Landau, M.,Engelberg, Y. (登録日: 2019-07-03, 公開日: 2020-08-19, 最終更新日: 2024-05-15)

主引用文献

Engelberg, Y.,Landau, M.
The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure.
Nat Commun, 11:3894-3894, 2020

PubMed Abstract: Here, we demonstrate the self-assembly of the antimicrobial human LL-37 active core (residues 17-29) into a protein fibril of densely packed helices. The surface of the fibril encompasses alternating hydrophobic and positively charged zigzagged belts, which likely underlie interactions with and subsequent disruption of negatively charged lipid bilayers, such as bacterial membranes. LL-37 correspondingly forms wide, ribbon-like, thermostable fibrils in solution, which co-localize with bacterial cells. Structure-guided mutagenesis analyses supports the role of self-assembly in antibacterial activity. LL-37 resembles, in sequence and in the ability to form amphipathic helical fibrils, the bacterial cytotoxic PSMα3 peptide that assembles into cross-α amyloid fibrils. This argues helical, self-assembling, basic building blocks across kingdoms of life and points to potential structural mimicry mechanisms. The findings expose a protein fibril which performs a biological activity, and offer a scaffold for functional and durable biomaterials for a wide range of medical and technological applications.

PubMed: 32753597
DOI: 10.1038/s41467-020-17736-x

実験手法

X-RAY DIFFRACTION (1.35 Å)