2M1P

[Aba5,14]BTD-2

2M1P の概要

• エントリーDOI: 10.2210/pdb2m1p/pdb
• 関連するPDBエントリー: 2lye
• NMR情報: BMRB: 18875
• 関連するBIRD辞書のPRD_ID: PRD_000941
• 分子名称: [Aba5,14]BTD-2 (1 entity in total)
• 機能のキーワード: theta-defensin, cyclic peptides, cyclic cystine ladder, disulfide bond, antimicrobial protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2054.59

構造登録者

Conibear, A.C.,Rosengren, K.,Daly, N.L.,Troiera Henriques, S.,Craik, D.J. (登録日: 2012-12-04, 公開日: 2013-02-27, 最終更新日: 2023-06-14)

主引用文献

Conibear, A.C.,Rosengren, K.J.,Daly, N.L.,Henriques, S.T.,Craik, D.J.
The cyclic cystine ladder in theta-defensins is important for structure and stability, but not antibacterial activity.
J.Biol.Chem., 288:10830-10840, 2013

PubMed Abstract: θ-Defensins are ribosomally synthesized cyclic peptides found in the leukocytes of some primate species and have promising applications as antimicrobial agents and scaffolds for peptide drugs. The cyclic cystine ladder motif, comprising a cyclic peptide backbone and three parallel disulfide bonds, is characteristic of θ-defensins. In this study, we explore the role of the cyclic peptide backbone and cystine ladder in the structure, stability, and activity of θ-defensins. θ-Defensin analogues with different numbers and combinations of disulfide bonds were synthesized and characterized in terms of their NMR solution structures, serum and thermal stabilities, and their antibacterial and membrane-binding activities. Whereas the structures and stabilities of the peptides were primarily dependent on the number and position of the disulfide bonds, their antibacterial and membrane-binding properties were dependent on the cyclic backbone. The results provide insights into the mechanism of action of θ-defensins and illustrate the potential of θ-defensin analogues as scaffolds for peptide drug design.

PubMed: 23430740
DOI: 10.1074/jbc.M113.451047

実験手法

SOLUTION NMR