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==CRYSTAL STRUCTURE OF THE LFW ECTODOMAIN OF THE PEPTIDOGLYCAN RECOGNITION PROTEIN LF== | |||
<StructureSection load='2xz8' size='340' side='right'caption='[[2xz8]], [[Resolution|resolution]] 1.94Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xz8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XZ8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xz8 OCA], [https://pdbe.org/2xz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xz8 RCSB], [https://www.ebi.ac.uk/pdbsum/2xz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xz8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PGPLF_DROME PGPLF_DROME] Peptidoglycan-recognition protein probably involved in innate immnunity by binding to peptidoglycans (PGN) of bacteria and activating the immune response. | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:21372849</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xz8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Basbous | [[Category: Large Structures]] | ||
[[Category: Coste | [[Category: Basbous N]] | ||
[[Category: Kellenberger | [[Category: Coste F]] | ||
[[Category: Leone | [[Category: Kellenberger C]] | ||
[[Category: Roussel | [[Category: Leone P]] | ||
[[Category: Royet | [[Category: Roussel A]] | ||
[[Category: Vincentelli | [[Category: Royet J]] | ||
[[Category: Vincentelli R]] | |||
Latest revision as of 13:42, 20 December 2023
CRYSTAL STRUCTURE OF THE LFW ECTODOMAIN OF THE PEPTIDOGLYCAN RECOGNITION PROTEIN LFCRYSTAL STRUCTURE OF THE LFW ECTODOMAIN OF THE PEPTIDOGLYCAN RECOGNITION PROTEIN LF
Structural highlights
FunctionPGPLF_DROME Peptidoglycan-recognition protein probably involved in innate immnunity by binding to peptidoglycans (PGN) of bacteria and activating the immune response. Publication Abstract from PubMedThe 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
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