3QTE

Crystal structure of human alpha-defensin 6 (H27W mutant)

3QTE の概要

• エントリーDOI: 10.2210/pdb3qte/pdb
• 関連するPDBエントリー: 1ZMP 1ZMQ
• 分子名称: Defensin-6, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: antimicrobial protein, paneth cells defensin, hd6, human alpha defensin
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: Q01524
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 15232.47

構造登録者

Pazgier, M.,Lu, W. (登録日: 2011-02-22, 公開日: 2012-01-11, 最終更新日: 2024-10-16)

主引用文献

Chu, H.,Pazgier, M.,Jung, G.,Nuccio, S.P.,Castillo, P.A.,de Jong, M.F.,Winter, M.G.,Winter, S.E.,Wehkamp, J.,Shen, B.,Salzman, N.H.,Underwood, M.A.,Tsolis, R.M.,Young, G.M.,Lu, W.,Lehrer, R.I.,Baumler, A.J.,Bevins, C.L.
Human alpha-defensin 6 promotes mucosal innate immunity through self-assembled peptide nanonets.
Science, 337:477-481, 2012

PubMed Abstract: Defensins are antimicrobial peptides that contribute broadly to innate immunity, including protection of mucosal tissues. Human α-defensin (HD) 6 is highly expressed by secretory Paneth cells of the small intestine. However, in contrast to the other defensins, it lacks appreciable bactericidal activity. Nevertheless, we report here that HD6 affords protection against invasion by enteric bacterial pathogens in vitro and in vivo. After stochastic binding to bacterial surface proteins, HD6 undergoes ordered self-assembly to form fibrils and nanonets that surround and entangle bacteria. This self-assembly mechanism occurs in vivo, requires histidine-27, and is consistent with x-ray crystallography data. These findings support a key role for HD6 in protecting the small intestine against invasion by diverse enteric pathogens and may explain the conservation of HD6 throughout Hominidae evolution.

PubMed: 22722251
DOI: 10.1126/science.1218831

実験手法

X-RAY DIFFRACTION (1.949 Å)