View source for 8xdg


==Cryo-EM structure of zebrafish urea transporter.==
<StructureSection load='8xdg' size='340' side='right'caption='[[8xdg]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xdg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XDG 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]] 3.1&#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=8xdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xdg OCA], [https://pdbe.org/8xdg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xdg RCSB], [https://www.ebi.ac.uk/pdbsum/8xdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xdg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A8M9Q878_DANRE A0A8M9Q878_DANRE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Urea's transmembrane transport through urea transporters (UT) is a fundamental physiological behavior for life activities. Here, we present 11 cryo-EM structures of four UT members in resting states, urea transport states, or inactive states bound with synthetic competitive, uncompetitive or noncompetitive inhibitor. Our results indicate that the binding of urea via a conserved urea recognition motif (URM) and the urea transport via H-bond transfer along the Q(Pb)-T(5b)-T(5a)-Q(Pa) motif among different UT members. Moreover, distinct binding modes of the competitive inhibitors 25a and ATB3, the uncompetitive inhibitor CF11 and the noncompetitive inhibitor HQA2 provide different mechanisms for blocking urea transport and achieved selectivity through L-P pocket, UCBP region and SCG pocket, respectively. In summary, our study not only allows structural understanding of urea transport via UTs but also afforded a structural landscape of hUT-A2 inhibition by competitive, uncompetitive and noncompetitive inhibitors, which may facilitate developing selective human UT-A inhibitors as a new class of salt-sparing diuretics.

Structural insights into the mechanisms of urea permeation and distinct inhibition modes of urea transporters.,Huang SM, Huang ZZ, Liu L, Xiong MY, Zhang C, Cai BY, Wang MW, Cai K, Jia YL, Wang JL, Zhang MH, Xie YH, Li M, Zhang H, Weng CH, Wen X, Li Z, Sun Y, Yi F, Yang Z, Xiao P, Yang F, Yu X, Tie L, Yang BX, Sun JP Nat Commun. 2024 Nov 26;15(1):10226. doi: 10.1038/s41467-024-54305-y. PMID:39587082<ref>PMID:39587082</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8xdg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Danio rerio]]
[[Category: Large Structures]]
[[Category: Huang S]]
[[Category: Liu L]]
[[Category: Sun J]]