5uar: Difference between revisions

<table><tr><td colspan='2'>[[5uar]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5tsi 5tsi]. 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://proteopedia.org/fgij/fg.htm?mol=5UAR FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cftr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</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://proteopedia.org/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>

[[http://www.uniprot.org/uniprot/Q1LX78_DANRE Q1LX78_DANRE]] Involved in the transport of chloride ions.[RuleBase:RU362037]

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.

 

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>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 5uar" style="background-color:#fffaf0;"></div>

[[Category: Brachidanio rerio]]

[[Category: Channel-conductance-controlling ATPase]]

[[Category: Chen, J]]

[[Category: Zhang, Z]]

[[Category: Membrane protein]]