7pmy
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==HsPepT2 bound to Ala-Phe in the inward facing partially occluded conformation== | |
| + | <StructureSection load='7pmy' size='340' side='right'caption='[[7pmy]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7pmy]] 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=7PMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PMY 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]] 3.8Å</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=7pmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pmy OCA], [https://pdbe.org/7pmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pmy RCSB], [https://www.ebi.ac.uk/pdbsum/7pmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pmy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/S15A2_HUMAN S15A2_HUMAN] Proton-coupled intake of oligopeptides of 2 to 4 amino acids with a preference for dipeptides (PubMed:7756356). Transports the dipeptide-like aminopeptidase inhibitor bestatin (By similarity). Can also transport the aminocephalosporin antibiotic cefadroxil (By similarity).[UniProtKB:P46029][UniProtKB:Q63424]<ref>PMID:7756356</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | [Figure: see text]. | ||
| - | + | Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes.,Killer M, Wald J, Pieprzyk J, Marlovits TC, Low C Sci Adv. 2021 Nov 5;7(45):eabk3259. doi: 10.1126/sciadv.abk3259. Epub 2021 Nov 3. PMID:34730990<ref>PMID:34730990</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7pmy" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Marlovits | + | __TOC__ |
| - | [[Category: Wald | + | </StructureSection> |
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Killer M]] | ||
| + | [[Category: Loew C]] | ||
| + | [[Category: Marlovits TC]] | ||
| + | [[Category: Pieprzyk J]] | ||
| + | [[Category: Wald J]] | ||
Current revision
HsPepT2 bound to Ala-Phe in the inward facing partially occluded conformation
| |||||||||||
Categories: Homo sapiens | Large Structures | Killer M | Loew C | Marlovits TC | Pieprzyk J | Wald J
