View source for 3odn


==The crystal structure of Drosophila Dally-Like Protein core domain==
<StructureSection load='3odn' size='340' side='right'caption='[[3odn]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3odn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ODN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ODN FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dlp, CG32146 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3odn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3odn OCA], [https://pdbe.org/3odn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3odn RCSB], [https://www.ebi.ac.uk/pdbsum/3odn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3odn ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/Q9GPL5_DROME Q9GPL5_DROME]] Cell surface proteoglycan that bears heparan sulfate (By similarity).[RuleBase:RU003519] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glypicans are heparan sulfate proteoglycans that modulate the signaling of multiple growth factors active during animal development, and loss of glypican function is associated with widespread developmental abnormalities. Glypicans consist of a conserved, approximately 45-kDa N-terminal protein core region followed by a stalk region that is tethered to the cell membrane by a glycosyl-phosphatidylinositol anchor. The stalk regions are predicted to be random coil but contain a variable number of attachment sites for heparan sulfate chains. Both the N-terminal protein core and the heparan sulfate attachments are important for glypican function. We report here the 2.4-A crystal structure of the N-terminal protein core region of the Drosophila glypican Dally-like (Dlp). This structure reveals an elongated, alpha-helical fold for glypican core regions that does not appear homologous to any known structure. The Dlp core protein is required for normal responsiveness to Hedgehog (Hh) signals, and we identify a localized region on the Dlp surface important for mediating its function in Hh signaling. Purified Dlp protein core does not, however, interact appreciably with either Hh or an Hh:Ihog complex.

Structure of the protein core of the glypican Dally-like and localization of a region important for hedgehog signaling.,Kim MS, Saunders AM, Hamaoka BY, Beachy PA, Leahy DJ Proc Natl Acad Sci U S A. 2011 Aug 9;108(32):13112-7. Epub 2011 Jul 26. PMID:21828006<ref>PMID:21828006</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3odn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drome]]
[[Category: Large Structures]]
[[Category: Kim, M S]]
[[Category: Leahy, D J]]
[[Category: Alpha helical bundle]]
[[Category: Hedgehog signaling]]
[[Category: Hedgehog via co-immunoprecipitation]]
[[Category: Membrane protein]]