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'''Unreleased structure'''


The entry 4arr is ON HOLD  until Apr 26 2014
==Crystal structure of the N-terminal domain of Drosophila Toll receptor with the magic triangle I3C==
<StructureSection load='4arr' size='340' side='right'caption='[[4arr]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4arr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ARR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ARR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3C:5-AMINO-2,4,6-TRIIODOBENZENE-1,3-DICARBOXYLIC+ACID'>I3C</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4arn|4arn]]</div></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=4arr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4arr OCA], [https://pdbe.org/4arr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4arr RCSB], [https://www.ebi.ac.uk/pdbsum/4arr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4arr ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Generating high-quality crystals remains a bottleneck in biological and materials sciences. Here a counter-diffusion method was used to improve the X-ray diffraction quality of the N-terminal domain of Drosophila melanogaster Toll receptor crystals. It was observed that crystallization occurred with a peculiar pattern along the capillary resembling Liesegang bands; this phenomenon is described at both macroscopic and atomic levels. It was found that bands appeared for native protein as well as for co-crystals of magic triangle (I3C)-bound protein even though they crystallize in different space groups. Crystallization occurred with a linear recurrence independent of the precipitant concentration and a protein-specific spacing coefficient. Bandwidth varied along the capillary, oscillating between large precipitation areas and single crystals. The reported data suggest that repetitive patterns can be generated with biological macromolecules in the presence of sodium malonate as a crystallization agent. A comparison with typical Liesegang patterns and the possible mechanism underlying this phenomenon are discussed.


Authors: Gangloff, M., Gay, N.J.
Liesegang-like patterns of Toll crystals grown in gel.,Gangloff M, Moreno A, Gay NJ J Appl Crystallogr. 2013 Apr 1;46(Pt 2):337-345. Epub 2013 Feb 14. PMID:23596340<ref>PMID:23596340</ref>


Description: Crystal structure of the N-terminal domain of Drosophila Toll receptor with the magic triangle I3C
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4arr" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Variable lymphocyte receptor 3D structures|Variable lymphocyte receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Gangloff, M]]
[[Category: Gay, N J]]
[[Category: Cytokine receptor]]
[[Category: Embryonic development]]
[[Category: Immune system]]
[[Category: Innate immunity]]
[[Category: Leucine-rich repeat]]
[[Category: Lrr hybrid technology]]

Latest revision as of 08:44, 25 August 2022

Crystal structure of the N-terminal domain of Drosophila Toll receptor with the magic triangle I3CCrystal structure of the N-terminal domain of Drosophila Toll receptor with the magic triangle I3C

Structural highlights

4arr is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Generating high-quality crystals remains a bottleneck in biological and materials sciences. Here a counter-diffusion method was used to improve the X-ray diffraction quality of the N-terminal domain of Drosophila melanogaster Toll receptor crystals. It was observed that crystallization occurred with a peculiar pattern along the capillary resembling Liesegang bands; this phenomenon is described at both macroscopic and atomic levels. It was found that bands appeared for native protein as well as for co-crystals of magic triangle (I3C)-bound protein even though they crystallize in different space groups. Crystallization occurred with a linear recurrence independent of the precipitant concentration and a protein-specific spacing coefficient. Bandwidth varied along the capillary, oscillating between large precipitation areas and single crystals. The reported data suggest that repetitive patterns can be generated with biological macromolecules in the presence of sodium malonate as a crystallization agent. A comparison with typical Liesegang patterns and the possible mechanism underlying this phenomenon are discussed.

Liesegang-like patterns of Toll crystals grown in gel.,Gangloff M, Moreno A, Gay NJ J Appl Crystallogr. 2013 Apr 1;46(Pt 2):337-345. Epub 2013 Feb 14. PMID:23596340[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Gangloff M, Moreno A, Gay NJ. Liesegang-like patterns of Toll crystals grown in gel. J Appl Crystallogr. 2013 Apr 1;46(Pt 2):337-345. Epub 2013 Feb 14. PMID:23596340 doi:http://dx.doi.org/10.1107/S0021889812051606

4arr, resolution 3.00Å

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