2MDB

Tachyplesin I in the presence of lipopolysaccharide

2MDB の概要

• エントリーDOI: 10.2210/pdb2mdb/pdb
• NMR情報: BMRB: 11538
• 分子名称: Tachyplesin-1 (1 entity in total)
• 機能のキーワード: peptide/lps, antimicrobial protein
• 由来する生物種: Tachypleus tridentatus (Chinese horseshoe crab,Japanese horseshoe crab)
• 細胞内の位置: Secreted: P14213
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2272.81

構造登録者

Kushibiki, T.,Kamiya, M.,Aizawa, T.,Kumaki, Y.,Kikukawa, T.,Mizuguchi, M.,Demura, M.,Kawabata, S.I.,Kawano, K. (登録日: 2013-09-09, 公開日: 2014-02-19, 最終更新日: 2024-10-16)

主引用文献

Kushibiki, T.,Kamiya, M.,Aizawa, T.,Kumaki, Y.,Kikukawa, T.,Mizuguchi, M.,Demura, M.,Kawabata, S.I.,Kawano, K.
Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide.
Biochim.Biophys.Acta, 1844:527-534, 2014

PubMed Abstract: Lipopolysaccharide (LPS) is a major constituent of the outer membrane of Gram-negative bacteria and is the very first site of interactions with antimicrobial peptides (AMPs). In order to gain better insight into the interaction between LPS and AMPs, we determined the structure of tachyplesin I (TP I), an antimicrobial peptide derived from horseshoe crab, in its bound state with LPS and proposed the complex structure of TP I and LPS using a docking program. CD and NMR measurements revealed that binding to LPS slightly extends the two β-strands of TP I and stabilizes the whole structure of TP I. The fluorescence wavelength of an intrinsic tryptophan of TP I and fluorescence quenching in the presence or absence of LPS indicated that a tryptophan residue is incorporated into the hydrophobic environment of LPS. Finally, we succeeded in proposing a structural model for the complex of TP I and LPS by using a docking program. The calculated model structure suggested that the cationic residues of TP I interact with phosphate groups and saccharides of LPS, whereas hydrophobic residues interact with the acyl chains of LPS.

PubMed: 24389234
DOI: 10.1016/j.bbapap.2013.12.017

実験手法

SOLUTION NMR