View source for 4pd9


==Structure of vcCNT-7C8C bound to adenosine==
<StructureSection load='4pd9' size='340' side='right'caption='[[4pd9]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pd9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PD9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.096&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4pd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pd9 OCA], [https://pdbe.org/4pd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pd9 RCSB], [https://www.ebi.ac.uk/pdbsum/4pd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pd9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9KPL5_VIBCH Q9KPL5_VIBCH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Concentrative nucleoside transporters (CNTs) are responsible for cellular entry of nucleosides, which serve as precursors to nucleic acids and act as signaling molecules. CNTs also play a crucial role in the uptake of nucleoside-derived drugs, including anticancer and antiviral agents. Understanding how CNTs recognize and import their substrates could not only lead to a better understanding of nucleoside-related biological processes but also the design of nucleoside-derived drugs that can better reach their targets. Here we present a combination of x-ray crystallographic and equilibrium-binding studies probing the molecular origins of nucleoside and nucleoside drug selectivity of a CNT from Vibrio cholerae. We then used this information in chemically modifying an anticancer drug so that is better transported by and selective for a single human CNT subtype. This work provides proof of principle for utilizing transporter structural and functional information for the design of compounds that enter cells more efficiently and selectively.

Structural basis of nucleoside and nucleoside drug selectivity by concentrative nucleoside transporters.,Johnson ZL, Lee JH, Lee K, Lee M, Kwon DY, Hong J, Lee SY Elife. 2014 Jul 31:e03604. doi: 10.7554/eLife.03604. PMID:25082345<ref>PMID:25082345</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pd9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
[[Category: Johnson ZL]]
[[Category: Lee S-Y]]