2OX2

Structure of the cantionic, antimicrobial hexapeptide cyclo(RRWWFR) bound to DPC-micelles

2OX2 の概要

• エントリーDOI: 10.2210/pdb2ox2/pdb
• 関連するPDBエントリー: 1qvk 1qvl 1ski 1skk 1skl 2otq
• 分子名称: cRW2 peptide (1 entity in total)
• 機能のキーワード: antimicrobial, cationic peptide, antimicrobial protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1009.19

構造登録者

Appelt, C.,Wessolowski, A.,Soderhall, J.A.,Dathe, M.,Schmieder, P. (登録日: 2007-02-19, 公開日: 2007-12-25, 最終更新日: 2024-11-13)

主引用文献

Appelt, C.,Wessolowski, A.,Dathe, M.,Schmieder, P.
Structures of cyclic, antimicrobial peptides in a membrane-mimicking environment define requirements for activity.
J.Pept.Sci., 14:524-527, 2007

PubMed Abstract: New antimicrobial compounds are of major importance because of the growing problem of bacterial resistance. In this context, antimicrobial peptides have received a lot of attention. Their mechanism of action, however, is often obscure. Here, the structures of two cyclic, antimicrobial peptides from the family of arginine- and tryptophan-rich peptides determined in a membrane-mimicking environment are described. The sequence of the peptides has been obtained from a cyclic parent peptide by scrambling the amino acids. While the activity of the peptides is similar to that of the parent peptide, the structures are not. The peptides do, however, all adopt an amphiphilic structure. A comparison between the structures helps to define the requirements for the activity of these peptides.

PubMed: 17985394
DOI: 10.1002/psc.924

実験手法

SOLUTION NMR