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4pd9

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(New page: '''Unreleased structure''' The entry 4pd9 is ON HOLD Authors: Johnson, Z.L., Lee, S.-Y. Description:)
Current revision (07:15, 27 September 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4pd9 is ON HOLD
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==Structure of vcCNT-7C8C bound to adenosine==
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<StructureSection load='4pd9' size='340' side='right'caption='[[4pd9]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9KPL5_VIBCH Q9KPL5_VIBCH]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Johnson, Z.L., Lee, S.-Y.
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4pd9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
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[[Category: Johnson ZL]]
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[[Category: Lee S-Y]]

Current revision

Structure of vcCNT-7C8C bound to adenosine

PDB ID 4pd9

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