View source for 2xz4


==Crystal structure of the LFZ ectodomain of the peptidoglycan recognition protein LF==
<StructureSection load='2xz4' size='340' side='right'caption='[[2xz4]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2xz4]] 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=2XZ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XZ4 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]] 1.72&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=2xz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xz4 OCA], [https://pdbe.org/2xz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xz4 RCSB], [https://www.ebi.ac.uk/pdbsum/2xz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xz4 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2xz4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Basbous N]]
[[Category: Coste F]]
[[Category: Kellenberger C]]
[[Category: Leone P]]
[[Category: Roussel A]]
[[Category: Royet J]]
[[Category: Vincentelli R]]