4a0p

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[[Image:4a0p.png|left|200px]]
 
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==Crystal structure of LRP6P3E3P4E4==
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The line below this paragraph, containing "STRUCTURE_4a0p", creates the "Structure Box" on the page.
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<StructureSection load='4a0p' size='340' side='right'caption='[[4a0p]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[4a0p]] 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=4A0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A0P 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]] 1.9&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_4a0p| PDB=4a0p | SCENE= }}
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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=4a0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0p OCA], [https://pdbe.org/4a0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a0p RCSB], [https://www.ebi.ac.uk/pdbsum/4a0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a0p 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 protein 6 (LRP6), alongside Frizzled receptors, transduces Wnt signaling across the plasma membrane. The LRP6 ectodomain comprises four tandem beta-propeller-EGF-like domain (PE) pairs that harbor binding sites for Wnt morphogens and their antagonists including Dickkopf 1 (Dkk1). To understand how these multiple interactions are integrated, we combined crystallographic analysis of the third and fourth PE pairs with electron microscopy (EM) to determine the complete ectodomain structure. An extensive inter-pair interface, conserved for the first-to-second and third-to-fourth PE interactions, contributes to a compact platform-like architecture, which is disrupted by mutations implicated in developmental diseases. EM reconstruction of the LRP6 platform bound to chaperone Mesd exemplifies a binding mode spanning PE pairs. Cellular and binding assays identify overlapping Wnt3a- and Dkk1-binding surfaces on the third PE pair, consistent with steric competition, but also suggest a model in which the platform structure supports an interplay of ligands through multiple interaction sites.
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===CRYSTAL STRUCTURE OF LRP6P3E3P4E4===
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Structural and Functional Studies of LRP6 Ectodomain Reveal a Platform for Wnt Signaling.,Chen S, Bubeck D, Macdonald BT, Liang WX, Mao JH, Malinauskas T, Llorca O, Aricescu AR, Siebold C, He X, Jones EY Dev Cell. 2011 Oct 11. PMID:22000855<ref>PMID:22000855</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 4a0p" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 22000855 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22000855}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[4a0p]] is a 1 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=4A0P OCA].
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==Reference==
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<ref group="xtra">PMID:022000855</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Aricescu, A R.]]
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[[Category: Large Structures]]
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[[Category: Chen, S.]]
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[[Category: Aricescu AR]]
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[[Category: Jones, E Y.]]
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[[Category: Chen S]]
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[[Category: Malinauskas, T.]]
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[[Category: Jones EY]]
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[[Category: Siebold, C.]]
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[[Category: Malinauskas T]]
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[[Category: Dkk1]]
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[[Category: Siebold C]]
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[[Category: Lrp6]]
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[[Category: Mesd]]
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[[Category: Signaling]]
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[[Category: Wnt signalling]]
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[[Category: Wnt3a]]
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Current revision

Crystal structure of LRP6P3E3P4E4

PDB ID 4a0p

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