3qte | pdb_00003qte
Crystal structure of human alpha-defensin 6 (H27W mutant)
Structural highlights
FunctionDEF6_HUMAN Has very low antimicrobial activity against Gram-negative and Gram-positive bacteria. May protect cells against infection with HIV-1.[1] [2] Publication Abstract from PubMedDefensins are antimicrobial peptides that contribute broadly to innate immunity, including protection of mucosal tissues. Human alpha-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. Human alpha-defensin 6 promotes mucosal innate immunity through self-assembled peptide nanonets.,Chu H, Pazgier M, Jung G, Nuccio SP, Castillo PA, de Jong MF, Winter MG, Winter SE, Wehkamp J, Shen B, Salzman NH, Underwood MA, Tsolis RM, Young GM, Lu W, Lehrer RI, Baumler AJ, Bevins CL Science. 2012 Jul 27;337(6093):477-81. Epub 2012 Jun 21. PMID:22722251[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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