2MN3

Structure of Platypus 'Intermediate' Defensin-like Peptide (Int-DLP)

2MN3 の概要

• エントリーDOI: 10.2210/pdb2mn3/pdb
• 関連するPDBエントリー: 1b8w 1bnb 1zue
• NMR情報: BMRB: 19878
• 分子名称: Defensin-BvL (1 entity in total)
• 機能のキーワード: defensin-like peptide, platypus defensin, beta-defensin, intermediate-dlp, antimicrobial protein
• 由来する生物種: Ornithorhynchus anatinus (duck-billed platypus,duckbill platypus)
• 細胞内の位置: Secreted (By similarity): P0C8B1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5000.90

構造登録者

Torres, A.M.,Bansal, P.S.,Koh, J.M.S.,Pages, G.,Wu, M.J.,Kuchel, P.W. (登録日: 2014-03-27, 公開日: 2014-09-17, 最終更新日: 2024-10-30)

主引用文献

Torres, A.M.,Bansal, P.,Koh, J.M.,Pages, G.,Wu, M.J.,Kuchel, P.W.
Structure and antimicrobial activity of platypus 'intermediate' defensin-like peptide.
Febs Lett., 588:1821-1826, 2014

PubMed Abstract: The three-dimensional structure of a chemically synthesized peptide that we have called 'intermediate' defensin-like peptide (Int-DLP), from the platypus genome, was determined by nuclear magnetic resonance (NMR) spectroscopy; and its antimicrobial activity was investigated. The overall structural fold of Int-DLP was similar to that of the DLPs and β-defensins, however the presence of a third antiparallel β-strand makes its structure more similar to the β-defensins than the DLPs. Int-DLP displayed potent antimicrobial activity against Staphylococcus aureus and Pseudomonas aeruginosa. The four arginine residues at the N-terminus of Int-DLP did not affect the overall fold, but were important for its antimicrobial potency.

PubMed: 24694388
DOI: 10.1016/j.febslet.2014.03.044

実験手法

SOLUTION NMR