4arn
From Proteopedia
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| - | + | ==Crystal structure of the N-terminal domain of Drosophila Toll receptor== | |
| - | === | + | <StructureSection load='4arn' size='340' side='right' caption='[[4arn]], [[Resolution|resolution]] 2.41Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4arn]] is a 4 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=4ARN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ARN FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=4arn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4arn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4arn RCSB], [http://www.ebi.ac.uk/pdbsum/4arn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Drosophila melanogaster Toll is the founding member of an important family of pathogen-recognition receptors in humans, the Toll-like receptor (TLR) family. In contrast, the prototypical receptor is a cytokine-like receptor for Spatzle (Spz) protein and plays a dual role in both development and immunity. Here, we present the crystal structure of the N-terminal domain of the receptor that encompasses the first 201 amino acids at 2.4 A resolution. To our knowledge, the cysteine-rich cap adopts a novel fold unique to Toll-1 orthologs in insects and that is not critical for ligand binding. However, we observed that an antibody directed against the first ten LRRs blocks Spz signaling in a Drosophila cell-based assay. Supplemented by point mutagenesis and deletion analysis, our data suggests that the region up to LRR 14 is involved in Spz binding. Comparison with mammalian TLRs reconciles previous contradictory findings about the mechanism of Toll activation. | ||
| - | + | Functional insights from the crystal structure of the N-terminal domain of the prototypical toll receptor.,Gangloff M, Arnot CJ, Lewis M, Gay NJ Structure. 2013 Jan 8;21(1):143-53. doi: 10.1016/j.str.2012.11.003. Epub 2012 Dec, 13. PMID:23245851<ref>PMID:23245851</ref> | |
| - | + | ||
| - | [[Category: Gangloff, M | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | [[Category: Gay, N J | + | </div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drome]] | ||
| + | [[Category: Gangloff, M]] | ||
| + | [[Category: Gay, N J]] | ||
[[Category: Cytokine receptor]] | [[Category: Cytokine receptor]] | ||
[[Category: Embryonic development]] | [[Category: Embryonic development]] | ||
Revision as of 09:16, 21 December 2014
Crystal structure of the N-terminal domain of Drosophila Toll receptor
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