6yv1
From Proteopedia
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==Structure of human b(0,+)AT1== | ==Structure of human b(0,+)AT1== | ||
| - | <StructureSection load='6yv1' size='340' side='right'caption='[[6yv1]]' scene=''> | + | <StructureSection load='6yv1' size='340' side='right'caption='[[6yv1]], [[Resolution|resolution]] 3.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YV1 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6yv1]] is a 1 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=6YV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YV1 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</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=6yv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yv1 OCA], [https://pdbe.org/6yv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yv1 RCSB], [https://www.ebi.ac.uk/pdbsum/6yv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yv1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [https://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 == | ||
| + | [https://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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Heteromeric amino acid transporters (HATs) comprise a group of membrane proteins that belong to the solute carrier (SLC) superfamily. They are formed by two different protein components: a light chain subunit from an SLC7 family member and a heavy chain subunit from the SLC3 family. The light chain constitutes the transport subunit whereas the heavy chain mediates trafficking to the plasma membrane and maturation of the functional complex. Mutation, malfunction, and dysregulation of HATs are associated with a wide range of pathologies or represent the direct cause of inherited and acquired disorders. Here we report the cryogenic electron microscopy structure of the neutral and basic amino acid transport complex (b([0,+])AT1-rBAT) which reveals a heterotetrameric protein assembly composed of two heavy and light chain subunits, respectively. The previously uncharacterized interaction between two HAT units is mediated via dimerization of the heavy chain subunits and does not include participation of the light chain subunits. The b((0,+))AT1 transporter adopts a LeuT fold and is captured in an inward-facing conformation. We identify an amino-acid-binding pocket that is formed by transmembrane helices 1, 6, and 10 and conserved among SLC7 transporters. | ||
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| + | Structural basis for amino acid exchange by a human heteromeric amino acid transporter.,Wu D, Grund TN, Welsch S, Mills DJ, Michel M, Safarian S, Michel H Proc Natl Acad Sci U S A. 2020 Sep 1;117(35):21281-21287. doi:, 10.1073/pnas.2008111117. Epub 2020 Aug 17. PMID:32817565<ref>PMID:32817565</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6yv1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Michel H]] | [[Category: Michel H]] | ||
[[Category: Safarian S]] | [[Category: Safarian S]] | ||
[[Category: Wu D]] | [[Category: Wu D]] | ||
Current revision
Structure of human b(0,+)AT1
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