7pmx: Difference between revisions

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'''Unreleased structure'''


The entry 7pmx is ON HOLD
==HsPepT1 bound to Ala-Phe in the outward facing open conformation==
<StructureSection load='7pmx' size='340' side='right'caption='[[7pmx]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7pmx]] 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=7PMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PMX 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]] 3.5&#8491;</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=7pmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pmx OCA], [https://pdbe.org/7pmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pmx RCSB], [https://www.ebi.ac.uk/pdbsum/7pmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pmx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/S15A1_HUMAN S15A1_HUMAN] Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides (PubMed:7896779, PubMed:18367661, PubMed:19685173). Primarily responsible for the absorption of dietary di- and tripeptides from the small intestinal lumen (By similarity).[UniProtKB:P36836]<ref>PMID:18367661</ref> <ref>PMID:19685173</ref> <ref>PMID:7896779</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
[Figure: see text].


Authors: Killer, M., Wald, J., Pieprzyk, J., Marlovits, T.C., Loew, C.
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>


Description: HsPepT1 bound to Ala-Phe in the outward facing open conformation
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Loew, C]]
<div class="pdbe-citations 7pmx" style="background-color:#fffaf0;"></div>
[[Category: Pieprzyk, J]]
== References ==
[[Category: Killer, M]]
<references/>
[[Category: Marlovits, T.C]]
__TOC__
[[Category: Wald, J]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Killer M]]
[[Category: Loew C]]
[[Category: Marlovits TC]]
[[Category: Pieprzyk J]]
[[Category: Wald J]]

Latest revision as of 12:33, 17 July 2024

HsPepT1 bound to Ala-Phe in the outward facing open conformation

7pmx, resolution 3.50Å

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