5uar: Difference between revisions

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'''Unreleased structure'''


The entry 5uar is ON HOLD
==Dephosphorylated, ATP-free cystic fibrosis transmembrane conductance regulator (CFTR) from zebrafish==
<StructureSection load='5uar' size='340' side='right' caption='[[5uar]], [[Resolution|resolution]] 3.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5uar]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UAR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UAR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D10:DECANE'>D10</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uak|5uak]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5uar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uar OCA], [http://pdbe.org/5uar PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uar RCSB], [http://www.ebi.ac.uk/pdbsum/5uar PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uar ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/Q1LX78_DANRE Q1LX78_DANRE]] Involved in the transport of chloride ions.[RuleBase:RU362037]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel evolved from the ATP-binding cassette (ABC) transporter family. In this study, we determined the structure of zebrafish CFTR in the absence of ATP by electron cryo-microscopy to 3.7 A resolution. Human and zebrafish CFTR share 55% sequence identity, and 42 of the 46 cystic-fibrosis-causing missense mutational sites are identical. In CFTR, we observe a large anion conduction pathway lined by numerous positively charged residues. A single gate near the extracellular surface closes the channel. The regulatory domain, dephosphorylated, is located in the intracellular opening between the two nucleotide-binding domains (NBDs), preventing NBD dimerization and channel opening. The structure also reveals why many cystic-fibrosis-causing mutations would lead to defects either in folding, ion conduction, or gating and suggests new avenues for therapeutic intervention.


Authors: Zhang, Z., Chen, J.
Atomic Structure of the Cystic Fibrosis Transmembrane Conductance Regulator.,Zhang Z, Chen J Cell. 2016 Dec 1;167(6):1586-1597.e9. doi: 10.1016/j.cell.2016.11.014. PMID:27912062<ref>PMID:27912062</ref>


Description: Dephosphorylated, ATP-free cystic fibrosis transmembrane conductance regulator (CFTR) from zebrafish
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5uar" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Channel-conductance-controlling ATPase]]
[[Category: Chen, J]]
[[Category: Zhang, Z]]
[[Category: Zhang, Z]]
[[Category: Chen, J]]
[[Category: Abc transporter]]
[[Category: Anion channel]]
[[Category: Cystic fibrosis]]
[[Category: Hydrolase]]
[[Category: Membrane protein]]

Revision as of 16:08, 18 January 2017

Dephosphorylated, ATP-free cystic fibrosis transmembrane conductance regulator (CFTR) from zebrafish

5uar, resolution 3.73Å

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