6li9

<table><tr><td colspan='2'>[[6li9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LI9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LI9 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PH:1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE'>3PH</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SLC3A1, RBAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SLC7A9, BAT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6li9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6li9 OCA], [http://pdbe.org/6li9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6li9 RCSB], [http://www.ebi.ac.uk/pdbsum/6li9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6li9 ProSAT]</span></td></tr>

== Disease ==

[[http://www.uniprot.org/uniprot/SLC31_HUMAN SLC31_HUMAN]] Cystinuria type A;2p21 microdeletion syndrome;Atypical hypotonia-cystinuria syndrome;Hypotonia-cystinuria syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Hypotonia-cystinuria syndrome is a contiguous gene syndrome caused by a homozygous deletion on chromosome 2p21 that disrupts the gene represented in this entry and PREPL (PubMed:16385448, PubMed:21686663). A homozygous 77.4-kb deletion that disrupts the gene represented in this entry, PREPL, and CAMKMT, causes atypical hypotonia-cystinuria syndrome, characterized by mild to moderate mental retardation and respiratory chain complex IV deficiency (PubMed:21686663).<ref>PMID:16385448</ref> <ref>PMID:21686663</ref> [[http://www.uniprot.org/uniprot/BAT1_HUMAN BAT1_HUMAN]] Cystinuria type B. The disease is caused by mutations affecting the gene represented in this entry.

== Function ==

[[http://www.uniprot.org/uniprot/SLC31_HUMAN SLC31_HUMAN]] Involved in the high-affinity, sodium-independent transport of cystine and neutral and dibasic amino acids (system B(0,+)-like activity). May function as an activator of SLC7A9 and be involved in the high-affinity reabsorption of cystine in the kidney tubule.<ref>PMID:11318953</ref> <ref>PMID:7686906</ref> <ref>PMID:8486766</ref> <ref>PMID:8663184</ref> [[http://www.uniprot.org/uniprot/BAT1_HUMAN BAT1_HUMAN]] Involved in the high-affinity, sodium-independent transport of cystine and neutral and dibasic amino acids (system b(0,+)-like activity). Thought to be responsible for the high-affinity reabsorption of cystine in the kidney tubule.<ref>PMID:10471498</ref> <ref>PMID:10588648</ref> <ref>PMID:16609684</ref>

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== Publication Abstract from PubMed ==

Heteromeric amino acid transporters (HATs) catalyze the transmembrane movement of amino acids, comprising two subunits, a heavy chain and a light chain, linked by a disulfide bridge. The b(0,+)AT (SLC7A9) is a representative light chain of HATs, forming heterodimer with rBAT, a heavy chain which mediates the membrane trafficking of b(0,+)AT. The b(0,+)AT-rBAT complex is an obligatory exchanger, which mediates the influx of cystine and cationic amino acids and the efflux of neutral amino acids in kidney and small intestine. Here, we report the cryo-EM structure of the human b(0,+)AT-rBAT complex alone and in complex with arginine substrate at resolution of 2.7 and 2.3 A, respectively. The overall structure of b(0,+)AT-rBAT exists as a dimer of heterodimer consistent with the previous study. A ligand molecule is bound to the substrate binding pocket, near which an occluded pocket is identified, to which we found that it is important for substrate transport.

Cryo-EM structure of the human heteromeric amino acid transporter b(0,+)AT-rBAT.,Yan R, Li Y, Shi Y, Zhou J, Lei J, Huang J, Zhou Q Sci Adv. 2020 Apr 15;6(16):eaay6379. doi: 10.1126/sciadv.aay6379. eCollection, 2020 Apr. PMID:32494597<ref>PMID:32494597</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Human]]

[[Category: Lei, J L]]

[[Category: Li, Y N]]

[[Category: Yan, R H]]

[[Category: Zhou, Q]]

[[Category: Transporter]]