4io4: Difference between revisions
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==Crystal Structure of the AvGluR1 ligand binding domain complex with serine at 1.94 Angstrom resolution== | ==Crystal Structure of the AvGluR1 ligand binding domain complex with serine at 1.94 Angstrom resolution== | ||
<StructureSection load='4io4' size='340' side='right' caption='[[4io4]], [[Resolution|resolution]] 1.94Å' scene=''> | <StructureSection load='4io4' size='340' side='right'caption='[[4io4]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4io4]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4io4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Adineta_vaga Adineta vaga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IO4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.941Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4io4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4io4 OCA], [https://pdbe.org/4io4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4io4 RCSB], [https://www.ebi.ac.uk/pdbsum/4io4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4io4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/E9P5T5_ADIVA E9P5T5_ADIVA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4io4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4io4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Adineta vaga]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Chittori S]] | ||
[[Category: | [[Category: Lomash S]] | ||
[[Category: | [[Category: Mayer ML]] | ||
Latest revision as of 18:27, 20 September 2023
Crystal Structure of the AvGluR1 ligand binding domain complex with serine at 1.94 Angstrom resolutionCrystal Structure of the AvGluR1 ligand binding domain complex with serine at 1.94 Angstrom resolution
Structural highlights
FunctionPublication Abstract from PubMedAvGluR1, a glutamate receptor ion channel from the primitive eukaryote Adineta vaga, is activated by alanine, cysteine, methionine, and phenylalanine, which produce lectin-sensitive desensitizing responses like those to glutamate, aspartate, and serine. AvGluR1 LBD crystal structures reveal an unusual scheme for binding dissimilar ligands that may be utilized by distantly related odorant/chemosensory receptors. Arginine residues in domain 2 coordinate the gamma-carboxyl group of glutamate, whereas in the alanine, methionine, and serine complexes a chloride ion acts as a surrogate ligand, replacing the gamma-carboxyl group. Removal of Cl lowers affinity for these ligands but not for glutamate or aspartate nor for phenylalanine, which occludes the anion binding site and binds with low affinity. AvGluR1 LBD crystal structures and sedimentation analysis also provide insights into the evolutionary link between prokaryotic and eukaryotic iGluRs and reveal features unique to both classes, emphasizing the need for additional structure-based studies on iGluR-ligand interactions. Anions Mediate Ligand Binding in Adineta vaga Glutamate Receptor Ion Channels.,Lomash S, Chittori S, Brown P, Mayer ML Structure. 2013 Mar 5;21(3):414-25. doi: 10.1016/j.str.2013.01.006. Epub 2013 Feb, 21. PMID:23434404[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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