5fb7

Ligand binding domain 2 of Penicillium marneffei MP1 protein complexed with multiple arachidonic acids

spinqualitylabelsall models 5fb7, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fb7 is a 4 chain structure with sequence from Talaromyces marneffei PM1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: ACD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A093VKV7_TALMA Publication Abstract from PubMed Talaromyces (Penicillium) marneffei is one of the leading causes of systemic mycosis in immunosuppressed or AIDS patients in Southeast Asia. How this intracellular pathogen evades the host immune defense remains unclear. We provide evidence that T. marneffei depletes levels of a key proinflammatory lipid mediator arachidonic acid (AA) to evade the host innate immune defense. Mechanistically, an abundant secretory mannoprotein Mp1p, shown previously to be a virulence factor, does so by binding AA with high affinity via a long hydrophobic central cavity found in the LBD2 domain. This sequesters a critical proinflammatory signaling lipid, and we see evidence that AA, AA's downstream metabolites, and the cytokines interleukin-6 and tumor necrosis factor alpha are downregulated in T. marneffei-infected J774 macrophages. Given that Mp1p-LBD2 homologs are identified in other fungal pathogens, we expect that this novel class of fatty-acid-binding proteins sequestering key proinflammatory lipid mediators represents a general virulence mechanism of pathogenic fungi. Talaromyces marneffei Mp1p Is a Virulence Factor that Binds and Sequesters a Key Proinflammatory Lipid to Dampen Host Innate Immune Response.,Sze KH, Lam WH, Zhang H, Ke YH, Tse MK, Woo PC, Lau SK, Lau CC, Cai JP, Tung ET, Lo RK, Xu S, Kao RY, Hao Q, Yuen KY Cell Chem Biol. 2017 Feb 16;24(2):182-194. doi: 10.1016/j.chembiol.2016.12.014., Epub 2017 Jan 19. PMID:28111099 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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