8cls: Difference between revisions
New page: '''Unreleased structure''' The entry 8cls is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Drosophila melanogaster insulin receptor ectodomain in complex with DILP5== | ||
<StructureSection load='8cls' size='340' side='right'caption='[[8cls]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8cls]] is a 8 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=8CLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CLS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</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=8cls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cls OCA], [https://pdbe.org/8cls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cls RCSB], [https://www.ebi.ac.uk/pdbsum/8cls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cls ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The insulin-related hormones regulate key life processes in Metazoa, from metabolism to growth, lifespan and aging, through an evolutionarily conserved insulin signalling axis (IIS). In humans the IIS axis is controlled by insulin, two insulin-like growth factors, two isoforms of the insulin receptor (hIR-A and -B), and its homologous IGF-1R. In Drosophila, this signalling engages seven insulin-like hormones (DILP1-7) and a single receptor (dmIR). This report describes the cryoEM structure of the dmIR ectodomain:DILP5 complex, revealing high structural homology between dmIR and hIR. The excess of DILP5 yields dmIR complex in an asymmetric 'T' conformation, similar to that observed in some complexes of human IRs. However, dmIR binds three DILP5 molecules in a distinct arrangement, showing also dmIR-specific features. This work adds structural support to evolutionary conservation of the IIS axis at the IR level, and also underpins a better understanding of an important model organism. | |||
Structural conservation of insulin/IGF signalling axis at the insulin receptors level in Drosophila and humans.,Viola CM, Frittmann O, Jenkins HT, Shafi T, De Meyts P, Brzozowski AM Nat Commun. 2023 Oct 7;14(1):6271. doi: 10.1038/s41467-023-41862-x. PMID:37805602<ref>PMID:37805602</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8cls" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | |||
[[Category: Large Structures]] | |||
[[Category: Brzozowski AM]] | |||
[[Category: Shafi T]] | |||
[[Category: Viola CM]] | |||
Latest revision as of 12:31, 17 October 2024
Drosophila melanogaster insulin receptor ectodomain in complex with DILP5Drosophila melanogaster insulin receptor ectodomain in complex with DILP5
Structural highlights
Publication Abstract from PubMedThe insulin-related hormones regulate key life processes in Metazoa, from metabolism to growth, lifespan and aging, through an evolutionarily conserved insulin signalling axis (IIS). In humans the IIS axis is controlled by insulin, two insulin-like growth factors, two isoforms of the insulin receptor (hIR-A and -B), and its homologous IGF-1R. In Drosophila, this signalling engages seven insulin-like hormones (DILP1-7) and a single receptor (dmIR). This report describes the cryoEM structure of the dmIR ectodomain:DILP5 complex, revealing high structural homology between dmIR and hIR. The excess of DILP5 yields dmIR complex in an asymmetric 'T' conformation, similar to that observed in some complexes of human IRs. However, dmIR binds three DILP5 molecules in a distinct arrangement, showing also dmIR-specific features. This work adds structural support to evolutionary conservation of the IIS axis at the IR level, and also underpins a better understanding of an important model organism. Structural conservation of insulin/IGF signalling axis at the insulin receptors level in Drosophila and humans.,Viola CM, Frittmann O, Jenkins HT, Shafi T, De Meyts P, Brzozowski AM Nat Commun. 2023 Oct 7;14(1):6271. doi: 10.1038/s41467-023-41862-x. PMID:37805602[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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