6FEY

Crystal structure of Drosophila neural ectodermal development factor Imp-L2 with Drosophila DILP5 insulin

6FEY の概要

• エントリーDOI: 10.2210/pdb6fey/pdb
• 関連するPDBエントリー: 2WFV 4CBP
• 分子名称: Neural/ectodermal development factor IMP-L2, Probable insulin-like peptide 5, ... (4 entities in total)
• 機能のキーワード: insulin, insulin binding protein, drosophila, imaginal morphogenesis, peptide binding protein
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 132417.45

構造登録者

Brzozowski, A.M.,Kulahin, N.,Kristensen, O.,Schluckebier, G.,Meyts, P.D. (登録日: 2018-01-03, 公開日: 2018-09-26, 最終更新日: 2024-10-23)

主引用文献

Roed, N.K.,Viola, C.M.,Kristensen, O.,Schluckebier, G.,Norrman, M.,Sajid, W.,Wade, J.D.,Andersen, A.S.,Kristensen, C.,Ganderton, T.R.,Turkenburg, J.P.,De Meyts, P.,Brzozowski, A.M.
Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones.
Nat Commun, 9:3860-3860, 2018

PubMed Abstract: 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.

PubMed: 30242155
DOI: 10.1038/s41467-018-06192-3

実験手法

X-RAY DIFFRACTION (3.48 Å)