2N30

Structure of Ace-pvhct-NH2

2N30 の概要

• エントリーDOI: 10.2210/pdb2n30/pdb
• NMR情報: BMRB: 25631
• 分子名称: Hemocyanin subunit L2 (1 entity in total)
• 機能のキーワード: antifungal protein
• 由来する生物種: Litopenaeus vannamei (white Pacific shrimp,white shrimp)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2782.10

構造登録者

Petit, V.W.,Rolland, J.,Blond, A.,Djediat, C.,Peduzzi, J.,Goulard, C.,Bachere, E.,Dupont, J.,Destoumieux-Garzon, D.,Rebuffat, S. (登録日: 2015-05-19, 公開日: 2015-06-17, 最終更新日: 2024-11-27)

主引用文献

Petit, V.W.,Rolland, J.L.,Blond, A.,Cazevieille, C.,Djediat, C.,Peduzzi, J.,Goulard, C.,Bachere, E.,Dupont, J.,Destoumieux-Garzon, D.,Rebuffat, S.
A hemocyanin-derived antimicrobial peptide from the penaeid shrimp adopts an alpha-helical structure that specifically permeabilizes fungal membranes.
Biochim.Biophys.Acta, 1860:557-568, 2015

PubMed Abstract: Hemocyanins are respiratory proteins with multiple functions. In diverse crustaceans hemocyanins can release histidine-rich antimicrobial peptides in response to microbial challenge. In penaeid shrimp, strictly antifungal peptides are released from the C-terminus of hemocyanins.

PubMed: 26708991
DOI: 10.1016/j.bbagen.2015.12.010

実験手法

SOLUTION NMR