View source for 2wfu


==Crystal structure of DILP5 variant DB==
<StructureSection load='2wfu' size='340' side='right'caption='[[2wfu]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wfu]] is a 2 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=2WFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WFU 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]] 1.85&#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=2wfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfu OCA], [https://pdbe.org/2wfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wfu RCSB], [https://www.ebi.ac.uk/pdbsum/2wfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/INSL5_DROME INSL5_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report the crystal structure of two variants of Drosophila melanogaster insulin-like peptide 5 (DILP5) at a resolution of 1.85 A. DILP5 shares the basic fold of the insulin peptide family (T conformation) but with a disordered B-chain C terminus. DILP5 dimerizes in the crystal and in solution. The dimer interface is not similar to that observed in vertebrates, i.e. through an anti-parallel beta-sheet involving the B-chain C termini but, in contrast, is formed through an anti-parallel beta-sheet involving the B-chain N termini. DILP5 binds to and activates the human insulin receptor and lowers blood glucose in rats. It also lowers trehalose levels in Drosophila. Reciprocally, human insulin binds to the Drosophila insulin receptor and induces negative cooperativity as in the human receptor. DILP5 also binds to insect insulin-binding proteins. These results show high evolutionary conservation of the insulin receptor binding properties despite divergent insulin dimerization mechanisms.

Structural and biological properties of the Drosophila insulin-like peptide 5 show evolutionary conservation.,Sajid W, Kulahin N, Schluckebier G, Ribel U, Henderson HR, Tatar M, Hansen BF, Svendsen AM, Kiselyov VV, Norgaard P, Wahlund PO, Brandt J, Kohanski RA, Andersen AS, De Meyts P J Biol Chem. 2011 Jan 7;286(1):661-73. Epub 2010 Oct 25. PMID:20974844<ref>PMID:20974844</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2wfu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: De Meyts P]]
[[Category: Kulahin N]]
[[Category: Sajid W]]
[[Category: Schluckebier G]]