Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Basbous N, Coste F, Leone P, Vincentelli R, Royet J, Kellenberger C, Roussel A. The Drosophila peptidoglycan-recognition protein LF interacts with peptidoglycan-recognition protein LC to downregulate the Imd pathway. EMBO Rep. 2011 Apr 1;12(4):327-33. Epub 2011 Mar 4. PMID:21372849 doi:10.1038/embor.2011.19
