4x82: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4x82]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X82 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4x82]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X82 FirstGlance]. <br> | ||
</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=4x82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x82 OCA], [http://pdbe.org/4x82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x82 RCSB], [http://www.ebi.ac.uk/pdbsum/4x82 PDBsum]</span></td></tr> | </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=4x82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x82 OCA], [http://pdbe.org/4x82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x82 RCSB], [http://www.ebi.ac.uk/pdbsum/4x82 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x82 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ZIP zinc transporter family is responsible for zinc uptake from the extracellular milieu or intracellular vesicles. The LIV-1 subfamily, containing nine out of the 14 human ZIP proteins, is featured with a large extracellular domain (ECD). The critical role of the ECD is manifested by disease-causing mutations on ZIP4, a representative LIV-1 protein. Here we report the first crystal structure of a mammalian ZIP4-ECD, which reveals two structurally independent subdomains and an unprecedented dimer centred at the signature PAL motif. Structure-guided mutagenesis, cell-based zinc uptake assays and mapping of the disease-causing mutations indicate that the two subdomains play pivotal but distinct roles and that the bridging region connecting them is particularly important for ZIP4 function. These findings lead to working hypotheses on how ZIP4-ECD exerts critical functions in zinc transport. The conserved dimeric architecture in ZIP4-ECD is also demonstrated to be a common structural feature among the LIV-1 proteins. | |||
Structural insights of ZIP4 extracellular domain critical for optimal zinc transport.,Zhang T, Sui D, Hu J Nat Commun. 2016 Jun 20;7:11979. doi: 10.1038/ncomms11979. PMID:27321477<ref>PMID:27321477</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4x82" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:53, 18 October 2017
Crystal Structure of the Extracellular Domain of ZIP4Crystal Structure of the Extracellular Domain of ZIP4
Structural highlights
Publication Abstract from PubMedThe ZIP zinc transporter family is responsible for zinc uptake from the extracellular milieu or intracellular vesicles. The LIV-1 subfamily, containing nine out of the 14 human ZIP proteins, is featured with a large extracellular domain (ECD). The critical role of the ECD is manifested by disease-causing mutations on ZIP4, a representative LIV-1 protein. Here we report the first crystal structure of a mammalian ZIP4-ECD, which reveals two structurally independent subdomains and an unprecedented dimer centred at the signature PAL motif. Structure-guided mutagenesis, cell-based zinc uptake assays and mapping of the disease-causing mutations indicate that the two subdomains play pivotal but distinct roles and that the bridging region connecting them is particularly important for ZIP4 function. These findings lead to working hypotheses on how ZIP4-ECD exerts critical functions in zinc transport. The conserved dimeric architecture in ZIP4-ECD is also demonstrated to be a common structural feature among the LIV-1 proteins. Structural insights of ZIP4 extracellular domain critical for optimal zinc transport.,Zhang T, Sui D, Hu J Nat Commun. 2016 Jun 20;7:11979. doi: 10.1038/ncomms11979. PMID:27321477[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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