4arn: Difference between revisions
No edit summary |
No edit summary |
||
| (8 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==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 [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Eptatretus_burgeri Eptatretus burgeri]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4ARN 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]] 2.41Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4arn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4arn OCA], [https://pdbe.org/4arn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4arn RCSB], [https://www.ebi.ac.uk/pdbsum/4arn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4arn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TOLL_DROME TOLL_DROME] [https://www.uniprot.org/uniprot/Q4G1L2_EPTBU Q4G1L2_EPTBU] | |||
<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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4arn" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Variable lymphocyte receptor 3D structures|Variable lymphocyte receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | |||
[[Category: Eptatretus burgeri]] | |||
[[Category: Large Structures]] | |||
[[Category: Gangloff M]] | |||
[[Category: Gay NJ]] | |||
Latest revision as of 14:33, 20 December 2023
Crystal structure of the N-terminal domain of Drosophila Toll receptorCrystal structure of the N-terminal domain of Drosophila Toll receptor
Structural highlights
FunctionPublication Abstract from PubMedDrosophila 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||