6qeu

Gga-AvBD11 (Avian beta-defensin 11 from Gallus gallus)

spinqualitylabelsall models 6qeu Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qeu is a 1 chain structure with sequence from Gallus gallus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 10 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLL11_CHICK Has bactericidal activity. Publication Abstract from PubMed Out of the 14 avian beta-defensins identified in the Gallus gallus genome, only 3 are present in the chicken egg, including the egg-specific avian beta-defensin 11 (Gga-AvBD11). Given its specific localization and its established antibacterial activity, Gga-AvBD11 appears to play a protective role in embryonic development. Gga-AvBD11 is an atypical double-sized defensin, predicted to possess 2 motifs related to beta-defensins and 6 disulfide bridges. The 3-dimensional NMR structure of the purified Gga-AvBD11 is a compact fold composed of 2 packed beta-defensin domains. This fold is the archetype of a structural family, dubbed herein as avian-double-beta-defensins (Av-DBD). We speculate that AvBD11 emanated from a monodomain gene ancestor and that similar events might have occurred in arthropods, leading to another structural family of less compact DBDs. We show that Gga-AvBD11 displays antimicrobial activities against gram-positive and gram-negative bacterial pathogens, the avian protozoan Eimeria tenella, and avian influenza virus. Gga-AvBD11 also shows cytotoxic and antiinvasive activities, suggesting that it may not only be involved in innate protection of the chicken embryo, but also in the (re)modeling of embryonic tissues. Finally, the contribution of either of the 2 Gga-AvBD11 domains to these biological activities was assessed, using chemically synthesized peptides. Our results point to a critical importance of the cationic N-terminal domain in mediating antibacterial, antiparasitic, and antiinvasive activities, with the C-terminal domain potentiating the 2 latter activities. Strikingly, antiviral activity in infected chicken cells, accompanied by marked cytotoxicity, requires the full-length protein. Structure, function, and evolution of Gga-AvBD11, the archetype of the structural avian-double-beta-defensin family.,Guyot N, Meudal H, Trapp S, Iochmann S, Silvestre A, Jousset G, Labas V, Reverdiau P, Loth K, Herve V, Aucagne V, Delmas AF, Rehault-Godbert S, Landon C Proc Natl Acad Sci U S A. 2019 Dec 23. pii: 1912941117. doi:, 10.1073/pnas.1912941117. PMID:31871151 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Defensin 3D structures

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