7cko: Difference between revisions
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==== | ==Cryo-EM structure of the human MCT1/Basigin-2 complex in the presence of anti-cancer drug candidate 7ACC2 in the inward-open conformation== | ||
<StructureSection load='7cko' size='340' side='right'caption='[[7cko]]' scene=''> | <StructureSection load='7cko' size='340' side='right'caption='[[7cko]], [[Resolution|resolution]] 2.95Å' 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= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7cko]] 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=7CKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CKO FirstGlance]. <br> | ||
</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=7cko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cko OCA], [https://pdbe.org/7cko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cko RCSB], [https://www.ebi.ac.uk/pdbsum/7cko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cko ProSAT]</span></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]] 2.95Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G5L:7-[methyl-(phenylmethyl)amino]-2-oxidanylidene-chromene-3-carboxylic+acid'>G5L</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=7cko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cko OCA], [https://pdbe.org/7cko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cko RCSB], [https://www.ebi.ac.uk/pdbsum/7cko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cko ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Disease == | |||
[https://www.uniprot.org/uniprot/MOT1_HUMAN MOT1_HUMAN] Metabolic myopathy due to lactate transporter defect;Ketoacidosis due to monocarboxylate transporter-1 deficiency;Exercise-induced hyperinsulinism. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MOT1_HUMAN MOT1_HUMAN] Bidirectional proton-coupled monocarboxylate transporter (PubMed:12946269, PubMed:33333023, PubMed:32946811). Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH (PubMed:12946269, PubMed:33333023). The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (By similarity). Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart (PubMed:32946811). Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 309-Asp is essential for the conformational transition (PubMed:33333023).[UniProtKB:P53986][UniProtKB:P53987]<ref>PMID:12946269</ref> <ref>PMID:32946811</ref> <ref>PMID:33333023</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Jiang X]] | ||
[[Category: Lei J]] | |||
[[Category: Wang N]] | |||
[[Category: Yan C]] | |||
[[Category: Yuan Y]] | |||
[[Category: Zhang S]] | |||
[[Category: Zhu A]] | |||