6fey: Difference between revisions
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<StructureSection load='6fey' size='340' side='right' caption='[[6fey]], [[Resolution|resolution]] 3.48Å' scene=''> | <StructureSection load='6fey' size='340' side='right' caption='[[6fey]], [[Resolution|resolution]] 3.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6fey]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FEY FirstGlance]. <br> | <table><tr><td colspan='2'>[[6fey]] is a 12 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=6FEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FEY FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cbp|4cbp]], [[2wfv|2wfv]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cbp|4cbp]], [[2wfv|2wfv]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ImpL2, CG15009 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Ilp5, HDC09365, CG33273 ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fey OCA], [http://pdbe.org/6fey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fey RCSB], [http://www.ebi.ac.uk/pdbsum/6fey PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fey ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fey OCA], [http://pdbe.org/6fey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fey RCSB], [http://www.ebi.ac.uk/pdbsum/6fey PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fey ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/IMPL2_DROME IMPL2_DROME]] Essential developmental role during embryogenesis, in particular the normal development of the nervous system. May be involved in some aspect of cell adhesion. | [[http://www.uniprot.org/uniprot/IMPL2_DROME IMPL2_DROME]] Essential developmental role during embryogenesis, in particular the normal development of the nervous system. May be involved in some aspect of cell adhesion. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The insulin/insulin-like growth factor signalling axis is an evolutionary ancient and highly conserved hormonal system involved in the regulation of metabolism, growth and lifespan in animals. Human insulin is stored in the pancreas, while insulin-like growth factor-1 (IGF-1) is maintained in blood in complexes with IGF-binding proteins (IGFBP1-6). Insect insulin-like polypeptide binding proteins (IBPs) have been considered as IGFBP-like structural and functional homologues. Here, we report structures of the Drosophila IBP Imp-L2 in its free form and bound to Drosophila insulin-like peptide 5 and human IGF-1. Imp-L2 contains two immunoglobulin-like fold domains and its architecture is unrelated to human IGFBPs, suggesting a distinct strategy for bioavailability regulation of insulin-like hormones. Similar hormone binding modes may exist in other insect vectors, as the IBP sequences are highly conserved. Therefore, these findings may open research routes towards a rational interference of transmission of diseases such as malaria, dengue and yellow fevers. | |||
Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones.,Roed NK, Viola CM, Kristensen O, Schluckebier G, Norrman M, Sajid W, Wade JD, Andersen AS, Kristensen C, Ganderton TR, Turkenburg JP, De Meyts P, Brzozowski AM Nat Commun. 2018 Sep 21;9(1):3860. doi: 10.1038/s41467-018-06192-3. PMID:30242155<ref>PMID:30242155</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6fey" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Drome]] | |||
[[Category: Brzozowski, A M]] | [[Category: Brzozowski, A M]] | ||
[[Category: Kristensen, O]] | [[Category: Kristensen, O]] | ||
Revision as of 11:50, 3 October 2018
Crystal structure of Drosophila neural ectodermal development factor Imp-L2 with Drosophila DILP5 insulinCrystal structure of Drosophila neural ectodermal development factor Imp-L2 with Drosophila DILP5 insulin
Structural highlights
Function[IMPL2_DROME] Essential developmental role during embryogenesis, in particular the normal development of the nervous system. May be involved in some aspect of cell adhesion. Publication Abstract from PubMedThe insulin/insulin-like growth factor signalling axis is an evolutionary ancient and highly conserved hormonal system involved in the regulation of metabolism, growth and lifespan in animals. Human insulin is stored in the pancreas, while insulin-like growth factor-1 (IGF-1) is maintained in blood in complexes with IGF-binding proteins (IGFBP1-6). Insect insulin-like polypeptide binding proteins (IBPs) have been considered as IGFBP-like structural and functional homologues. Here, we report structures of the Drosophila IBP Imp-L2 in its free form and bound to Drosophila insulin-like peptide 5 and human IGF-1. Imp-L2 contains two immunoglobulin-like fold domains and its architecture is unrelated to human IGFBPs, suggesting a distinct strategy for bioavailability regulation of insulin-like hormones. Similar hormone binding modes may exist in other insect vectors, as the IBP sequences are highly conserved. Therefore, these findings may open research routes towards a rational interference of transmission of diseases such as malaria, dengue and yellow fevers. Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones.,Roed NK, Viola CM, Kristensen O, Schluckebier G, Norrman M, Sajid W, Wade JD, Andersen AS, Kristensen C, Ganderton TR, Turkenburg JP, De Meyts P, Brzozowski AM Nat Commun. 2018 Sep 21;9(1):3860. doi: 10.1038/s41467-018-06192-3. PMID:30242155[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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