View source for 4ykj


==Mnemiopsis leidyi ML032222a iGluR LBD complex with Alanine==
<StructureSection load='4ykj' size='340' side='right'caption='[[4ykj]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ykj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mnemiopsis_leidyi Mnemiopsis leidyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YKJ 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]] 1.401&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</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=4ykj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ykj OCA], [https://pdbe.org/4ykj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ykj RCSB], [https://www.ebi.ac.uk/pdbsum/4ykj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ykj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0R4I973_MNELE A0A0R4I973_MNELE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Recent genome projects for ctenophores have revealed the presence of numerous ionotropic glutamate receptors (iGluRs) in Mnemiopsis leidyi and Pleurobrachia bachei, among our earliest metazoan ancestors. Sequence alignments and phylogenetic analysis show that these form a distinct clade from the well-characterized AMPA, kainate, and NMDA iGluR subtypes found in vertebrates. Although annotated as glutamate and kainate receptors, crystal structures of the ML032222a and PbiGluR3 ligand-binding domains (LBDs) reveal endogenous glycine in the binding pocket, whereas ligand-binding assays show that glycine binds with nanomolar affinity; biochemical assays and structural analysis establish that glutamate is occluded from the binding cavity. Further analysis reveals ctenophore-specific features, such as an interdomain Arg-Glu salt bridge, present only in subunits that bind glycine, but also a conserved disulfide in loop 1 of the LBD that is found in all vertebrate NMDA but not AMPA or kainate receptors. We hypothesize that ctenophore iGluRs are related to an early ancestor of NMDA receptors, suggesting a common evolutionary path for ctenophores and bilaterian species, and suggest that future work should consider both glycine and glutamate as candidate neurotransmitters in ctenophore species.

Glycine activated ion channel subunits encoded by ctenophore glutamate receptor genes.,Alberstein R, Grey R, Zimmet A, Simmons DK, Mayer ML Proc Natl Acad Sci U S A. 2015 Nov 3;112(44):E6048-57. doi:, 10.1073/pnas.1513771112. Epub 2015 Oct 12. PMID:26460032<ref>PMID:26460032</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ykj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mnemiopsis leidyi]]
[[Category: Alberstein RG]]
[[Category: Mayer ML]]