2xz8: Difference between revisions

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<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=2xz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xz8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xz8 RCSB], [http://www.ebi.ac.uk/pdbsum/2xz8 PDBsum]</span></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=2xz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xz8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xz8 RCSB], [http://www.ebi.ac.uk/pdbsum/2xz8 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://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.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 19:10, 25 December 2014

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

2xz8 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.
Ligands:, ,
Resources:FirstGlance, OCA, RCSB, PDBsum

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

  1. 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

2xz8, resolution 1.94Å

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