View source for 4kma


==Crystal structure of Drosophila Suppressor of Fused==
<StructureSection load='4kma' size='340' side='right'caption='[[4kma]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kma]] 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=4KMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KMA 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]] 2.68&#8491;</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=4kma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kma OCA], [https://pdbe.org/4kma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kma RCSB], [https://www.ebi.ac.uk/pdbsum/4kma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kma ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9VG38_DROME Q9VG38_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hedgehog (Hh) signalling regulates embryonic development and adult tissue homoeostasis. Mutations of its pathway components including Suppressor of Fused (Sufu) and Gli/Ci predispose to cancers and congenital anomalies. The Sufu-Gli protein complex occupies a central position in the vertebrate Hh signalling pathway, especially in mammals. Here structures of full-length human and Drosophila Sufu, the human Sufu-Gli complex, along with normal mode analysis and FRET measurement results, reveal that Sufu alternates between 'open' and 'closed' conformations. The 'closed' form of Sufu is stabilized by Gli binding and inhibited by Hh treatment, whereas the 'open' state of Sufu is promoted by Gli-dissociation and Hh signalling. Mutations of critical interface residues disrupt the Sufu-Gli complex and prevent Sufu from repressing Gli-mediated transcription, tethering Gli in the cytoplasm and protecting Gli from the 26S proteasome-mediated degradation. Our study thus provides mechanistic insight into the mutual recognition and regulation between Sufu and Gli/Ci.

Structural insight into the mutual recognition and regulation between Suppressor of Fused and Gli/Ci.,Zhang Y, Fu L, Qi X, Zhang Z, Xia Y, Jia J, Jiang J, Zhao Y, Wu G Nat Commun. 2013;4:2608. doi: 10.1038/ncomms3608. PMID:24217340<ref>PMID:24217340</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kma" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Qi X]]
[[Category: Wu G]]
[[Category: Zhang Y]]
[[Category: Zhang Z]]