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7AL0

Crystal Structure of Heymonin, a Novel Frog-derived Peptide

7AL0 の概要
エントリーDOI10.2210/pdb7al0/pdb
分子名称Heymonin, CHLORIDE ION (3 entities in total)
機能のキーワードantimicrobial peptide, inflammation, microhyla heymonsivogt, antimicrobial protein
由来する生物種Microhyla heymonsi
タンパク質・核酸の鎖数1
化学式量合計4341.30
構造登録者
Kascakova, B.,Prudnikova, T.,Kuta Smatanova, I.,Xu, X. (登録日: 2020-10-03, 公開日: 2021-04-21, 最終更新日: 2024-10-23)
主引用文献Chai, J.,Chen, X.,Ye, T.,Zeng, B.,Zeng, Q.,Wu, J.,Kascakova, B.,Martins, L.A.,Prudnikova, T.,Smatanova, I.K.,Kotsyfakis, M.,Xu, X.
Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties.
Elife, 10:-, 2021
Cited by
PubMed Abstract: Antimicrobial peptides form part of the innate immune response and play a vital role in host defense against pathogens. Here we report a new antimicrobial peptide belonging to the cathelicidin family, cathelicidin-MH (cath-MH), from the skin of frog. Cath-MH has a single α-helical structure in membrane-mimetic environments and is antimicrobial against fungi and bacteria, especially Gram-negative bacteria. In contrast to other cathelicidins, cath-MH suppresses coagulation by affecting the enzymatic activities of tissue plasminogen activator, plasmin, β-tryptase, elastase, thrombin, and chymase. Cath-MH protects against lipopolysaccharide (LPS)- and cecal ligation and puncture-induced sepsis, effectively ameliorating multiorgan pathology and inflammatory cytokine through its antimicrobial, LPS-neutralizing, coagulation suppressing effects as well as suppression of MAPK signaling. Taken together, these data suggest that cath-MH is an attractive candidate therapeutic agent for the treatment of septic shock.
PubMed: 33875135
DOI: 10.7554/eLife.64411
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 7al0
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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