4krr: Difference between revisions
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New page: '''Unreleased structure''' The entry 4krr is ON HOLD Authors: Chu, M.L.-H., Choi, H.-J., Ahn, V.E., Daniels, D.L., Nusse, R., Weis, W.I. Description: Crystal structure of Drosophila Wn... |
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The | ==Crystal structure of Drosophila WntD N-terminal domain-linker (residues 31-240)== | ||
<StructureSection load='4krr' size='340' side='right'caption='[[4krr]], [[Resolution|resolution]] 2.12Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4krr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KRR 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]] 2.124Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=4krr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4krr OCA], [https://pdbe.org/4krr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4krr RCSB], [https://www.ebi.ac.uk/pdbsum/4krr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4krr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/WNT8_DROME WNT8_DROME] Binds as a ligand to a family of frizzled seven-transmembrane receptors and acts through a cascade of genes on the nucleus. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Wnts are secreted growth factors that have critical roles in cell fate determination and stem cell renewal. The Wnt/beta-catenin pathway is initiated by binding of a Wnt protein to a Frizzled (Fzd) receptor and a coreceptor, LDL receptor-related protein 5 or 6 (LRP5/6). We report the 2.1 A resolution crystal structure of a Drosophila WntD fragment encompassing the N-terminal domain and the linker that connects it to the C-terminal domain. Differences in the structures of WntD and Xenopus Wnt8, including the positions of a receptor-binding beta hairpin and a large solvent-filled cavity in the helical core, indicate conformational plasticity in the N-terminal domain that may be important for Wnt-Frizzled specificity. Structure-based mutational analysis of mouse Wnt3a shows that the linker between the N- and C-terminal domains is required for LRP6 binding. These findings provide important insights into Wnt function and evolution. | |||
Structural Studies of Wnts and Identification of an LRP6 Binding Site.,Chu ML, Ahn VE, Choi HJ, Daniels DL, Nusse R, Weis WI Structure. 2013 Jul 2;21(7):1235-42. doi: 10.1016/j.str.2013.05.006. Epub 2013, Jun 20. PMID:23791946<ref>PMID:23791946</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4krr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | |||
[[Category: Large Structures]] | |||
[[Category: Ahn VE]] | |||
[[Category: Choi H-J]] | |||
[[Category: Chu ML-H]] | |||
[[Category: Daniels DL]] | |||
[[Category: Nusse R]] | |||
[[Category: Weis WI]] | |||
