3QTE

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

Summary for 3QTE

• Entry DOI: 10.2210/pdb3qte/pdb
• Related: 1ZMP 1ZMQ
• Descriptor: Defensin-6, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: antimicrobial protein, paneth cells defensin, hd6, human alpha defensin
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: Q01524
• Total number of polymer chains: 4
• Total formula weight: 15232.47

Authors

Pazgier, M.,Lu, W. (deposition date: 2011-02-22, release date: 2012-01-11, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.949 Å)