8tzs: Difference between revisions

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'''Unreleased structure'''


The entry 8tzs is ON HOLD
==Structure of human WLS==
<StructureSection load='8tzs' size='340' side='right'caption='[[8tzs]], [[Resolution|resolution]] 3.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8tzs]] is a 1 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=8TZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TZS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.84&#8491;</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=8tzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tzs OCA], [https://pdbe.org/8tzs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tzs RCSB], [https://www.ebi.ac.uk/pdbsum/8tzs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tzs ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/WLS_HUMAN WLS_HUMAN] The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/WLS_HUMAN WLS_HUMAN] Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins (PubMed:34587386). Plays also an important role in establishment of the anterior-posterior body axis formation during development (By similarity).<ref>PMID:16678095</ref> <ref>PMID:16678096</ref> <ref>PMID:34587386</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Wnt proteins are enzymatically lipidated by Porcupine (PORCN) in the ER and bind to Wntless (WLS) for intracellular transport and secretion. Mechanisms governing the transfer of these low-solubility Wnts from the ER to the extracellular space remain unclear. Through structural and functional analyses of Wnt7a, a crucial Wnt involved in central nervous system angiogenesis and blood-brain barrier maintenance, we have elucidated the principles of Wnt biogenesis and Wnt7-specific signaling. The Wnt7a-WLS complex binds to calreticulin (CALR), revealing that CALR functions as a chaperone to facilitate Wnt transfer from PORCN to WLS during Wnt biogenesis. Our structures, functional analyses, and molecular dynamics simulations demonstrate that a phospholipid in the core of Wnt-bound WLS regulates the association and dissociation between Wnt and WLS, suggesting a lipid-mediated Wnt secretion mechanism. Finally, the structure of Wnt7a bound to RECK, a cell-surface Wnt7 co-receptor, reveals how RECK(CC4) engages the N-terminal domain of Wnt7a to activate Wnt7-specific signaling.


Authors:  
,  PMID:37852257<ref>PMID:37852257</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8tzs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Hu Q]]
[[Category: Li X]]
[[Category: Qi X]]