6xtz

<table><tr><td colspan='2'>[[6xtz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XTZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XTZ FirstGlance]. <br>

</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O18:[(2~{S})-2-azanyl-3-oxidanylidene-propyl]+(~{Z})-hexadec-9-enoate'>O18</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dlp, CG17703, CG5031, CT16138, D-gpcB, Dally-like, DLP, Dlp, Dly, dly, Dmel\CG32146, CG32146, Dmel_CG32146 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xtz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xtz OCA], [http://pdbe.org/6xtz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xtz RCSB], [http://www.ebi.ac.uk/pdbsum/6xtz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xtz ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/Q9VUG1_DROME Q9VUG1_DROME]] Cell surface proteoglycan that bears heparan sulfate.[RuleBase:RU003519]

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

A relatively small number of proteins have been suggested to act as morphogens-signalling molecules that spread within tissues to organize tissue repair and the specification of cell fate during development. Among them are Wnt proteins, which carry a palmitoleate moiety that is essential for signalling activity(1-3). How a hydrophobic lipoprotein can spread in the aqueous extracellular space is unknown. Several mechanisms, such as those involving lipoprotein particles, exosomes or a specific chaperone, have been proposed to overcome this so-called Wnt solubility problem(4-6). Here we provide evidence against these models and show that the Wnt lipid is shielded by the core domain of a subclass of glypicans defined by the Dally-like protein (Dlp). Structural analysis shows that, in the presence of palmitoleoylated peptides, these glypicans change conformation to create a hydrophobic space. Thus, glypicans of the Dlp family protect the lipid of Wnt proteins from the aqueous environment and serve as a reservoir from which Wnt proteins can be handed over to signalling receptors.

Glypicans shield the Wnt lipid moiety to enable signalling at a distance.,McGough IJ, Vecchia L, Bishop B, Malinauskas T, Beckett K, Joshi D, O'Reilly N, Siebold C, Jones EY, Vincent JP Nature. 2020 Jul 22. pii: 10.1038/s41586-020-2498-z. doi:, 10.1038/s41586-020-2498-z. PMID:32699409<ref>PMID:32699409</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 6xtz" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Drome]]

[[Category: Jones, E Y]]

[[Category: Vecchia, L]]

[[Category: Wnt]]