View source for 2rop


==Solution structure of domains 3 and 4 of human ATP7B==
<StructureSection load='2rop' size='340' side='right'caption='[[2rop]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rop]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ROP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ROP FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATP7B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4] </span></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=2rop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rop OCA], [https://pdbe.org/2rop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rop RCSB], [https://www.ebi.ac.uk/pdbsum/2rop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rop ProSAT]</span></td></tr>
</table>
== Disease ==
[[https://www.uniprot.org/uniprot/ATP7B_HUMAN ATP7B_HUMAN]] Defects in ATP7B are the cause of Wilson disease (WD) [MIM:[https://omim.org/entry/277900 277900]]. WD is an autosomal recessive disorder of copper metabolism in which copper cannot be incorporated into ceruloplasmin in liver, and cannot be excreted from the liver into the bile. Copper accumulates in the liver and subsequently in the brain and kidney. The disease is characterized by neurologic manifestations and signs of cirrhosis.<ref>PMID:8298641</ref> <ref>PMID:7626145</ref> <ref>PMID:8533760</ref> <ref>PMID:8938442</ref> <ref>PMID:8931691</ref> <ref>PMID:8782057</ref> <ref>PMID:9311736</ref> <ref>PMID:9772425</ref> <ref>PMID:9222767</ref> <ref>PMID:8980283</ref> <ref>PMID:9887381</ref> <ref>PMID:9482578</ref> <ref>PMID:9554743</ref> <ref>PMID:9452121</ref> <ref>PMID:9671269</ref> <ref>PMID:9829905</ref> <ref>PMID:10194254</ref> <ref>PMID:10447265</ref> <ref>PMID:10502776</ref> <ref>PMID:10502777</ref> <ref>PMID:10051024</ref> <ref>PMID:10544227</ref> <ref>PMID:10453196</ref> <ref>PMID:11216666</ref> <ref>PMID:11093740</ref> <ref>PMID:10790207</ref> <ref>PMID:10721669</ref> <ref>PMID:11043508</ref> <ref>PMID:11180609</ref> <ref>PMID:11690702</ref> <ref>PMID:11243728</ref> <ref>PMID:11954751</ref> <ref>PMID:12544487</ref> <ref>PMID:12325021</ref> <ref>PMID:12376745</ref> <ref>PMID:14986826</ref> <ref>PMID:14639035</ref> <ref>PMID:15024742</ref> <ref>PMID:15557537</ref> <ref>PMID:14966923</ref> <ref>PMID:15845031</ref> <ref>PMID:15811015</ref> <ref>PMID:15952988</ref> <ref>PMID:16207219</ref> <ref>PMID:16283883</ref> <ref>PMID:16088907</ref> <ref>PMID:15967699</ref> <ref>PMID:17718866</ref> <ref>PMID:18373411</ref> <ref>PMID:18203200</ref> <ref>PMID:21682854</ref>  
== Function ==
[[https://www.uniprot.org/uniprot/ATP7B_HUMAN ATP7B_HUMAN]] Involved in the export of copper out of the cells, such as the efflux of hepatic copper into the bile. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/2rop_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rop ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Wilson disease protein or ATP7B is a P 1B-type ATPase involved in human copper homeostasis. The extended N-terminus of ATP7B protrudes into the cytosol and contains six Cu(I) binding domains. This report presents the NMR structure of the polypeptide consisting of soluble Cu(I) binding domains 3 and 4. The two domains exhibit ferredoxin-like folds, are linked by a flexible loop, and act independently of one another. Domains 3 and 4 tend to aggregate in a concentration-dependent manner involving nonspecific intermolecular interactions. Both domains can be loaded with Cu(I) when provided as an acetonitrile complex or by the chaperone HAH1. HAH1 forms a 70% complex with domain 4 that is in fast exchange with the free protein in solution. The ability of HAH1 to form a complex only with some domains of ATP7B is an interesting property of this class of proteins and may have a signaling role in the function of the ATPases.

Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1.,Banci L, Bertini I, Cantini F, Rosenzweig AC, Yatsunyk LA Biochemistry. 2008 Jul 15;47(28):7423-9. Epub 2008 Jun 18. PMID:18558714<ref>PMID:18558714</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rop" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Copper-exporting ATPase]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Banci, L]]
[[Category: Bertini, I]]
[[Category: Cantini, F]]
[[Category: Rosenzweig, A C]]
[[Category: Yatsunyk, L A]]
[[Category: Alternative splicing]]
[[Category: Atp-binding]]
[[Category: Copper]]
[[Category: Copper transport]]
[[Category: Cytoplasm]]
[[Category: Disease mutation]]
[[Category: Golgi apparatus]]
[[Category: Hydrolase]]
[[Category: Ion transport]]
[[Category: Magnesium]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Mitochondrion]]
[[Category: Mobility]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: Polymorphism]]
[[Category: Protein-protein interaction]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Wilson protein]]