1HU7

SOLUTION STRUCTURE OF T7 NOVISPIRIN

1HU7 の概要

• エントリーDOI: 10.2210/pdb1hu7/pdb
• NMR情報: BMRB: 5034
• 分子名称: T7 NOVISPIRIN (1 entity in total)
• 機能のキーワード: solution structure, unknown function
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2258.84

構造登録者

Sawai, M.V.,Waring, A.J.,Kearney, W.R.,McCray Jr., P.B.,Forsyth, W.R.,Lehrer, R.I.,Tack, B.F. (登録日: 2001-01-04, 公開日: 2002-04-05, 最終更新日: 2024-05-22)

主引用文献

Sawai, M.V.,Waring, A.J.,Kearney, W.R.,McCray Jr., P.B.,Forsyth, W.R.,Lehrer, R.I.,Tack, B.F.
Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides.
Protein Eng., 15:225-232, 2002

PubMed Abstract: We studied three model antibacterial peptides that resembled the N-terminal 18 amino acids of SMAP-29, an alpha-helical, antimicrobial peptide of sheep. Although the parent compound, ovispirin-1 (KNLRR IIRKI IHIIK KYG), was potently antimicrobial, it was also highly cytotoxic to human epithelial cells and hemolytic for human erythrocytes. Single residue substitutions to ovispirin-1 yielded two substantially less cytotoxic peptides (novispirins), with intact antimicrobial properties. One of these, novispirin G-10, differed from ovispirin-1 only by containing glycine at position 10, instead of isoleucine. The other, novispirin T-7, contained threonine instead of isoleucine at position 7. We determined the three-dimensional solution structures of all three peptides by circular dichroism spectroscopy and two-dimensional nuclear magnetic resonance spectroscopy. Although all retained an amphipathic helical structure in 2,2,2-trifluoroethanol, they manifested subtle fine-structural changes that evidently impacted their activities greatly. These findings show that simple structural modifications can 'fine-tune' an antimicrobial peptide to minimize unwanted cytotoxicity while retaining its desired activity.

PubMed: 11932493
DOI: 10.1093/protein/15.3.225

実験手法

SOLUTION NMR