3s2k

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(New page: '''Unreleased structure''' The entry 3s2k is ON HOLD Authors: Ahn, V.E., Chu, M.L.-H., Choi, H.-J., Tran, D., Abo, A., Weis, W.I. Description: Structural basis of Wnt signaling inhibit...)
Current revision (10:25, 6 November 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3s2k is ON HOLD
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==Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.==
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<StructureSection load='3s2k' size='340' side='right'caption='[[3s2k]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3s2k]] 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=3S2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S2K FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=3s2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s2k OCA], [https://pdbe.org/3s2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s2k RCSB], [https://www.ebi.ac.uk/pdbsum/3s2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s2k ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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.
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling. The LRP5/6 ectodomain contains four beta-propeller/EGF-like domain repeats. The first two repeats, LRP6(1-2), bind to several Wnt variants, whereas LRP6(3-4) binds other Wnts. We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts. Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane. Thus, Wnts bound to either portion of the LRP6 ectodomain likely bear a similar spatial relationship to Frizzled coreceptors.
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Authors: Ahn, V.E., Chu, M.L.-H., Choi, H.-J., Tran, D., Abo, A., Weis, W.I.
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Structural Basis of Wnt Signaling Inhibition by Dickkopf Binding to LRP5/6.,Ahn VE, Chu ML, Choi HJ, Tran D, Abo A, Weis WI Dev Cell. 2011 Oct 12. PMID:22000856<ref>PMID:22000856</ref>
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Description: Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.
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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 3s2k" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Abo A]]
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[[Category: Ahn VE]]
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[[Category: Choi H-J]]
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[[Category: Chu ML-H]]
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[[Category: Tran D]]
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[[Category: Weis WI]]

Current revision

Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.

PDB ID 3s2k

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