4cqk
From Proteopedia
Crystal structure of ligand-bound NaD1
Structural highlights
FunctionDEF_NICAL Plant defense peptide with antifungal activity against F.oxysporum and B.cinerea. Retards the growth of the Lepidopteran insect pests H.armigera and H.punctigera. Publication Abstract from PubMedCationic antimicrobial peptides (CAPs) such as defensins are ubiquitously found innate immune molecules that often exhibit broad activity against microbial pathogens and mammalian tumor cells. Many CAPs act at the plasma membrane of cells leading to membrane destabilization and permeabilization. In this study, we describe a novel cell lysis mechanism for fungal and tumor cells by the plant defensin NaD1 that acts via direct binding to the plasma membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2). We determined the crystal structure of a NaD1:PIP2 complex, revealing a striking oligomeric arrangement comprising seven dimers of NaD1 that cooperatively bind the anionic headgroups of 14 PIP2 molecules through a unique 'cationic grip' configuration. Site-directed mutagenesis of NaD1 confirms that PIP2-mediated oligomerization is important for fungal and tumor cell permeabilization. These observations identify an innate recognition system by NaD1 for direct binding of PIP2 that permeabilizes cells via a novel membrane disrupting mechanism. DOI: http://dx.doi.org/10.7554/eLife.01808.001. Phosphoinositide-mediated oligomerization of a defensin induces cell lysis.,Poon IKh, Baxter AA, Lay FT, Mills GD, Adda CG, Payne JA, Phan TK, Ryan GF, White JA, Veneer PK, van der Weerden NL, Anderson MA, Kvansakul M, Hulett MD Elife. 2014 Apr 1;3:e01808. doi: 10.7554/eLife.01808. PMID:24692446[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Large Structures | Nicotiana alata | Baxter AA | Hulett MD | Kvansakul M | Lay FT | Mills GM | Poon IKH