3ODN

The crystal structure of Drosophila Dally-Like Protein core domain

3ODN の概要

• エントリーDOI: 10.2210/pdb3odn/pdb
• 分子名称: Dally-like protein (2 entities in total)
• 機能のキーワード: alpha helical bundle, hedgehog signaling, hedgehog via co-immunoprecipitation, membrane protein
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• 細胞内の位置: Cell membrane ; Lipid-anchor, GPI-anchor : Q9GPL5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57650.55

構造登録者

Kim, M.-S.,Leahy, D.J. (登録日: 2010-08-11, 公開日: 2011-07-27, 最終更新日: 2024-10-30)

主引用文献

Kim, M.S.,Saunders, A.M.,Hamaoka, B.Y.,Beachy, P.A.,Leahy, D.J.
Structure of the protein core of the glypican Dally-like and localization of a region important for hedgehog signaling.
Proc.Natl.Acad.Sci.USA, 108:13112-13117, 2011

PubMed Abstract: Glypicans are heparan sulfate proteoglycans that modulate the signaling of multiple growth factors active during animal development, and loss of glypican function is associated with widespread developmental abnormalities. Glypicans consist of a conserved, approximately 45-kDa N-terminal protein core region followed by a stalk region that is tethered to the cell membrane by a glycosyl-phosphatidylinositol anchor. The stalk regions are predicted to be random coil but contain a variable number of attachment sites for heparan sulfate chains. Both the N-terminal protein core and the heparan sulfate attachments are important for glypican function. We report here the 2.4-Å crystal structure of the N-terminal protein core region of the Drosophila glypican Dally-like (Dlp). This structure reveals an elongated, α-helical fold for glypican core regions that does not appear homologous to any known structure. The Dlp core protein is required for normal responsiveness to Hedgehog (Hh) signals, and we identify a localized region on the Dlp surface important for mediating its function in Hh signaling. Purified Dlp protein core does not, however, interact appreciably with either Hh or an Hh:Ihog complex.

PubMed: 21828006
DOI: 10.1073/pnas.1109877108

実験手法

X-RAY DIFFRACTION (2.4 Å)