3s8v: Difference between revisions

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[[Image:3s8v.png|left|200px]]


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==Crystal structure of LRP6-Dkk1 complex==
The line below this paragraph, containing "STRUCTURE_3s8v", creates the "Structure Box" on the page.
<StructureSection load='3s8v' size='340' side='right'caption='[[3s8v]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3s8v]] is a 3 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=3S8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S8V FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3s8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s8v OCA], [https://pdbe.org/3s8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s8v RCSB], [https://www.ebi.ac.uk/pdbsum/3s8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s8v ProSAT]</span></td></tr>
{{STRUCTURE_3s8v|  PDB=3s8v  |  SCENE= }}
</table>
== Disease ==
[https://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN] Coronary artery disease - hyperlipidemia - hypertension - diabetes - osteoporosis. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN] Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity).<ref>PMID:11448771</ref> <ref>PMID:11357136</ref> <ref>PMID:15778503</ref> <ref>PMID:16341017</ref> <ref>PMID:16513652</ref> <ref>PMID:17400545</ref> <ref>PMID:17326769</ref> <ref>PMID:19107203</ref> <ref>PMID:19801552</ref> <ref>PMID:19293931</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Low-density-lipoprotein (LDL) receptor-related proteins 5 and 6 (LRP5/6) are Wnt co-receptors essential for Wnt/beta-catenin signaling. Dickkopf 1 (DKK1) inhibits Wnt signaling by interacting with the extracellular domains of LRP5/6 and is a drug target for multiple diseases. Here we present the crystal structures of a human LRP6-E3E4-DKK1 complex and the first and second halves of human LRP6's four propeller-epidermal growth factor (EGF) pairs (LRP6-E1E2 and LRP6-E3E4). Combined with EM analysis, these data demonstrate that LRP6-E1E2 and LRP6-E3E4 form two rigid structural blocks, with a short intervening hinge that restrains their relative orientation. The C-terminal domain of DKK1 (DKK1c) interacts with the top surface of the LRP6-E3 YWTD propeller and given their structural similarity, probably also that of the LRP6-E1 propeller, through conserved hydrophobic patches buttressed by a network of salt bridges and hydrogen bonds. Our work provides key insights for understanding LRP5/6 structure and the interaction of LRP5/6 with DKK, as well as for drug discovery.


===Crystal structure of LRP6-Dkk1 complex===
Crystal structures of the extracellular domain of LRP6 and its complex with DKK1.,Cheng Z, Biechele T, Wei Z, Morrone S, Moon RT, Wang L, Xu W Nat Struct Mol Biol. 2011 Oct 9. doi: 10.1038/nsmb.2139. PMID:21984209<ref>PMID:21984209</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3s8v" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 21984209 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_21984209}}
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</StructureSection>
==About this Structure==
[[3s8v]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S8V OCA].
 
==Reference==
<ref group="xtra">PMID:021984209</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Cheng, Z.]]
[[Category: Large Structures]]
[[Category: Xu, W.]]
[[Category: Cheng Z]]
[[Category: Ldl receptor-like protein]]
[[Category: Xu W]]
[[Category: Lrp5]]
[[Category: Lrp6]]
[[Category: Receptor]]
[[Category: Signaling protein]]
[[Category: Wnt]]
[[Category: Ywtd b-propeller]]

Latest revision as of 08:09, 9 October 2024

Crystal structure of LRP6-Dkk1 complex

3s8v, resolution 3.10Å

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