2xz4 | pdb_00002xz4

Crystal structure of the LFZ ectodomain of the peptidoglycan recognition protein LF

spinqualitylabelsall models 2xz4, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xz4 is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.72Å Ligands: 1PG, CU, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PGPLF_DROME Peptidoglycan-recognition protein probably involved in innate immnunity by binding to peptidoglycans (PGN) of bacteria and activating the immune response. Publication Abstract from PubMed The peptidoglycan (PGN)-recognition protein LF (PGRP-LF) is a specific negative regulator of the immune deficiency (Imd) pathway in Drosophila. We determine the crystal structure of the two PGRP domains constituting the ectodomain of PGRP-LF at 1.72 and 1.94 A resolution. The structures show that the LFz and LFw domains do not have a PGN-docking groove that is found in other PGRP domains, and they cannot directly interact with PGN, as confirmed by biochemical-binding assays. By using surface plasmon resonance analysis, we show that the PGRP-LF ectodomain interacts with the PGRP-LCx ectodomain in the absence and presence of tracheal cytotoxin. Our results suggest a mechanism for downregulation of the Imd pathway on the basis of the competition between PRGP-LCa and PGRP-LF to bind to PGRP-LCx. The Drosophila peptidoglycan-recognition protein LF interacts with peptidoglycan-recognition protein LC to downregulate the Imd pathway.,Basbous N, Coste F, Leone P, Vincentelli R, Royet J, Kellenberger C, Roussel A EMBO Rep. 2011 Apr 1;12(4):327-33. Epub 2011 Mar 4. PMID:21372849 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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