8qey

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<table><tr><td colspan='2'>[[8qey]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QEY FirstGlance]. <br>
<table><tr><td colspan='2'>[[8qey]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QEY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AJP:Digitonin'>AJP</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AJP:(25R)-2beta,15alpha-dihydroxy-5beta,8alpha,10alpha,14beta,17beta-spirostan-3alpha-yl+beta-D-glucopyranosyl-(1- 3)-beta-D-galactopyranosyl-(1- 2)-[beta-D-xylopyranosyl-(1- 3)]-beta-D-glucopyranosyl-(1- 4)-beta-D-galactopyranoside'>AJP</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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=8qey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qey OCA], [https://pdbe.org/8qey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qey RCSB], [https://www.ebi.ac.uk/pdbsum/8qey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qey ProSAT]</span></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=8qey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qey OCA], [https://pdbe.org/8qey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qey RCSB], [https://www.ebi.ac.uk/pdbsum/8qey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qey ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/AAA1_HUMAN AAA1_HUMAN] Associates with SLC3A2/4F2hc to form a functional heterodimeric complex that translocates small neutral L- and D-amino acids across the plasma membrane. Preferentially mediates exchange transport, but can also operate via facilitated diffusion (By similarity) (PubMed:10863037). Acts as a major transporter for glycine, L- and D-serine in the central nervous system. At the spinal cord and brainstem regulates glycine metabolism and glycinergic inhibitory neurotransmission by providing for glycine de novo synthesis from L-serine and glycine recycling from astrocytes to glycinergic motor neurons (By similarity). At Schaffer collateral-CA1 synapses mediates D-serine and glycine release that modulates post-synaptic activation of NMDA receptors and excitatory glutamatergic transmission (By similarity). May regulate D-serine release from mesenchymal progenitors located in developing subcutaneous adipose tissue, favoring white adipocyte over thermogenic beige adipocyte lineage commitment (By similarity).[UniProtKB:P63115][UniProtKB:P63116]<ref>PMID:10863037</ref>
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== Publication Abstract from PubMed ==
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Recent cryoEM studies elucidated details of the structural basis for the substrate selectivity and translocation of heteromeric amino acid transporters. However, Asc1/CD98hc is the only neutral heteromeric amino acid transporter that can function through facilitated diffusion, and the only one that efficiently transports glycine and D-serine, and thus has a regulatory role in the central nervous system. Here we use cryoEM, ligand-binding simulations, mutagenesis, transport assays, and molecular dynamics to define human Asc1/CD98hc determinants for substrate specificity and gain insights into the mechanisms that govern substrate translocation by exchange and facilitated diffusion. The cryoEM structure of Asc1/CD98hc is determined at 3.4-3.8 A resolution, revealing an inward-facing semi-occluded conformation. We find that Ser 246 and Tyr 333 are essential for Asc1/CD98hc substrate selectivity and for the exchange and facilitated diffusion modes of transport. Taken together, these results reveal the structural bases for ligand binding and transport features specific to human Asc1.
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Structure and mechanisms of transport of human Asc1/CD98hc amino acid transporter.,Rullo-Tubau J, Martinez-Molledo M, Bartoccioni P, Puch-Giner I, Arias A, Saen-Oon S, Stephan-Otto Attolini C, Artuch R, Diaz L, Guallar V, Errasti-Murugarren E, Palacin M, Llorca O Nat Commun. 2024 Apr 6;15(1):2986. doi: 10.1038/s41467-024-47385-3. PMID:38582862<ref>PMID:38582862</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8qey" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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Revision as of 09:51, 17 October 2024

Structure of human Asc1/CD98hc heteromeric amino acid transporter

PDB ID 8qey

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