4my2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "4my2" [edit=sysop:move=sysop])
Current revision (10:17, 30 October 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 4my2 is ON HOLD
+
==Crystal Structure of Norrin in fusion with Maltose Binding Protein==
 +
<StructureSection load='4my2' size='340' side='right'caption='[[4my2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4my2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MY2 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]] 2.4&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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=4my2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4my2 OCA], [https://pdbe.org/4my2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4my2 RCSB], [https://www.ebi.ac.uk/pdbsum/4my2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4my2 ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/NDP_HUMAN NDP_HUMAN] Retinopathy of prematurity;Familial exudative vitreoretinopathy;Coats disease;Persistent hyperplastic primary vitreous;Norrie disease. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/NDP_HUMAN NDP_HUMAN] Activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. Plays a central role in retinal vascularization by acting as a ligand for FZD4 that signals via stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. Acts in concert with TSPAN12 to activate FZD4 independently of the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1). May be involved in a pathway that regulates neural cell differentiation and proliferation. Possible role in neuroectodermal cell-cell interaction.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Norrin is a cysteine-rich growth factor that is required for angiogenesis in the eye, ear, brain, and female reproductive organs. It functions as an atypical Wnt ligand by specifically binding to the Frizzled 4 (Fz4) receptor. Here we report the crystal structure of Norrin, which reveals a unique dimeric structure with each monomer adopting a conserved cystine knot fold. Functional studies demonstrate that the novel Norrin dimer interface is required for Fz4 activation. Furthermore, we demonstrate that Norrin contains separate binding sites for Fz4 and for the Wnt ligand coreceptor Lrp5 (low-density lipoprotein-related protein 5) or Lrp6. Instead of inducing Fz4 dimerization, Norrin induces the formation of a ternary complex with Fz4 and Lrp5/6 by binding to their respective extracellular domains. These results provide crucial insights into the assembly and activation of the Norrin-Fz4-Lrp5/6 signaling complex.
-
Authors: Ke, J., Jurecky, C., Chen, C., Gu, X., Parker, N., Williams, B.O., Melcher, K., Xu, H.E.
+
Structure and function of Norrin in assembly and activation of a Frizzled 4-Lrp5/6 complex.,Ke J, Harikumar KG, Erice C, Chen C, Gu X, Wang L, Parker N, Cheng Z, Xu W, Williams BO, Melcher K, Miller LJ, Xu HE Genes Dev. 2013 Nov 1;27(21):2305-19. doi: 10.1101/gad.228544.113. PMID:24186977<ref>PMID:24186977</ref>
-
Description: Crystal Structure of Norrin in fusion with Maltose Binding Protein
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 4my2" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Escherichia coli O157:H7]]
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Chen C]]
 +
[[Category: Gu X]]
 +
[[Category: Jurecky C]]
 +
[[Category: Ke J]]
 +
[[Category: Melcher K]]
 +
[[Category: Parker N]]
 +
[[Category: Williams BO]]
 +
[[Category: Xu HE]]

Current revision

Crystal Structure of Norrin in fusion with Maltose Binding Protein

PDB ID 4my2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4my2"
Personal tools