6y76

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Current revision (09:17, 9 October 2024) (edit) (undo)
 
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<StructureSection load='6y76' size='340' side='right'caption='[[6y76]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
<StructureSection load='6y76' size='340' side='right'caption='[[6y76]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6y76]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y76 FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y76 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=6y76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y76 OCA], [https://pdbe.org/6y76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y76 RCSB], [https://www.ebi.ac.uk/pdbsum/6y76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y76 ProSAT]</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=6y76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y76 OCA], [https://pdbe.org/6y76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y76 RCSB], [https://www.ebi.ac.uk/pdbsum/6y76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y76 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/TFR1_HUMAN TFR1_HUMAN] Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site.<ref>PMID:3568132</ref>
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== Publication Abstract from PubMed ==
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Supply of iron into human cells is achieved by iron carrier protein transferrin and its receptor that upon complex formation get internalized by endocytosis. Similarly, the iron needs to be delivered into the brain, and necessitates the transport across the blood-brain barrier. While there are still unanswered questions about these mechanisms, extensive efforts have been made to use the system for delivery of therapeutics into biological compartments. The dimeric form of the receptor, where each subunit consists of three domains, further complicates the detailed investigation of molecular determinants responsible for guiding the receptor interactions with other proteins. Especially the apical domain's biological function has been elusive. To further the study of transferrin receptor, we have computationally decoupled the apical domain for soluble expression, and validated the design strategy by structure determination. Besides presenting a methodology for solubilizing domains, the results will allow for study of apical domain's function.
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Computational backbone design enables soluble engineering of transferrin receptor apical domain.,Sjostrom DJ, Berger SA, Oberdorfer G, Bjelic S Proteins. 2020 Jun 26. doi: 10.1002/prot.25974. PMID:32592192<ref>PMID:32592192</ref>
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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 6y76" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Berger SA]]
[[Category: Berger SA]]
[[Category: Bjelic S]]
[[Category: Bjelic S]]
[[Category: Oberdorfer G]]
[[Category: Oberdorfer G]]
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[[Category: Sjostrom DJ]]
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[[Category: Sjorstrom D]]

Current revision

AP01 - a redesigned transferrin receptor apical domain

PDB ID 6y76

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OCA

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