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| | <StructureSection load='2f2l' size='340' side='right'caption='[[2f2l]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2f2l' size='340' side='right'caption='[[2f2l]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2f2l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F2L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2f2l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F2L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=HSQ:2-(ACETYLAMINO)-2-DEOXY-ALPHA-L-IDOPYRANOSE'>HSQ</scene>, <scene name='pdbligand=MLD:GLCNAC(BETA1-4)-MURNAC(1,6-ANHYDRO)-L-ALA-GAMMA-D-GLU-MESO-A2PM-D-ALA'>MLD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=HSQ:2-(ACETYLAMINO)-2-DEOXY-ALPHA-L-IDOPYRANOSE'>HSQ</scene>, <scene name='pdbligand=MLD:GLCNAC(BETA1-4)-MURNAC(1,6-ANHYDRO)-L-ALA-GAMMA-D-GLU-MESO-A2PM-D-ALA'>MLD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f2l OCA], [http://pdbe.org/2f2l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f2l RCSB], [http://www.ebi.ac.uk/pdbsum/2f2l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f2l ProSAT]</span></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=2f2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f2l OCA], [https://pdbe.org/2f2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f2l RCSB], [https://www.ebi.ac.uk/pdbsum/2f2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f2l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PGPLC_DROME PGPLC_DROME]] Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. Isoform a and isoform x mediate the induction by LPS and Gram-negative bacteria, while isoform x mediates the induction by peptidoglycan.<ref>PMID:11872802</ref> <ref>PMID:12777387</ref> <ref>PMID:16006509</ref> | + | [[https://www.uniprot.org/uniprot/PGPLC_DROME PGPLC_DROME]] Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. Isoform a and isoform x mediate the induction by LPS and Gram-negative bacteria, while isoform x mediates the induction by peptidoglycan.<ref>PMID:11872802</ref> <ref>PMID:12777387</ref> <ref>PMID:16006509</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[PGPLC_DROME] Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. Isoform a and isoform x mediate the induction by LPS and Gram-negative bacteria, while isoform x mediates the induction by peptidoglycan.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Tracheal cytotoxin (TCT), a naturally occurring fragment of Gram-negative peptidoglycan, is a potent elicitor of innate immune responses in Drosophila. It induces the heterodimerization of its recognition receptors, the peptidoglycan recognition proteins (PGRPs) LCa and LCx, which activates the immune deficiency pathway. The crystal structure at 2.1 angstrom resolution of TCT in complex with the ectodomains of PGRP-LCa and PGRP-LCx shows that TCT is bound to and presented by the LCx ectodomain for recognition by the LCa ectodomain; the latter lacks a canonical peptidoglycan-docking groove conserved in other PGRPs. The interface, revealed in atomic detail, between TCT and the receptor complex highlights the importance of the anhydro-containing disaccharide in bridging the two ectodomains together and the critical role of diaminopimelic acid as the specificity determinant for PGRP interaction.
Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor.,Chang CI, Chelliah Y, Borek D, Mengin-Lecreulx D, Deisenhofer J Science. 2006 Mar 24;311(5768):1761-4. PMID:16556841[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Choe KM, Werner T, Stoven S, Hultmark D, Anderson KV. Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila. Science. 2002 Apr 12;296(5566):359-62. Epub 2002 Feb 28. PMID:11872802 doi:http://dx.doi.org/10.1126/science.1070216
- ↑ Werner T, Borge-Renberg K, Mellroth P, Steiner H, Hultmark D. Functional diversity of the Drosophila PGRP-LC gene cluster in the response to lipopolysaccharide and peptidoglycan. J Biol Chem. 2003 Jul 18;278(29):26319-22. Epub 2003 May 30. PMID:12777387 doi:http://dx.doi.org/10.1074/jbc.C300184200
- ↑ Chang CI, Ihara K, Chelliah Y, Mengin-Lecreulx D, Wakatsuki S, Deisenhofer J. Structure of the ectodomain of Drosophila peptidoglycan-recognition protein LCa suggests a molecular mechanism for pattern recognition. Proc Natl Acad Sci U S A. 2005 Jul 19;102(29):10279-84. Epub 2005 Jul 8. PMID:16006509
- ↑ Chang CI, Chelliah Y, Borek D, Mengin-Lecreulx D, Deisenhofer J. Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor. Science. 2006 Mar 24;311(5768):1761-4. PMID:16556841 doi:311/5768/1761
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