5EO9

Crystal Structure of the complex of Dpr6 Domain 1 bound to DIP-alpha Domain 1+2

5EO9 の概要

• エントリーDOI: 10.2210/pdb5eo9/pdb
• 分子名称: Dpr6, isoform C, CG32791, isoform A, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: immunoglobulin superfamily, cell adhesion molecule, cell surface receptor, synapse formation, cell adhesion
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36910.47

構造登録者

Ozkan, E.,Zinn, K.,Garcia, K.C. (登録日: 2015-11-10, 公開日: 2016-01-06, 最終更新日: 2024-10-16)

主引用文献

Carrillo, R.A.,Ozkan, E.,Menon, K.P.,Nagarkar-Jaiswal, S.,Lee, P.T.,Jeon, M.,Birnbaum, M.E.,Bellen, H.J.,Garcia, K.C.,Zinn, K.
Control of Synaptic Connectivity by a Network of Drosophila IgSF Cell Surface Proteins.
Cell, 163:1770-1782, 2015

PubMed Abstract: We have defined a network of interacting Drosophila cell surface proteins in which a 21-member IgSF subfamily, the Dprs, binds to a nine-member subfamily, the DIPs. The structural basis of the Dpr-DIP interaction code appears to be dictated by shape complementarity within the Dpr-DIP binding interface. Each of the six dpr and DIP genes examined here is expressed by a unique subset of larval and pupal neurons. In the neuromuscular system, interactions between Dpr11 and DIP-γ affect presynaptic terminal development, trophic factor responses, and neurotransmission. In the visual system, dpr11 is selectively expressed by R7 photoreceptors that use Rh4 opsin (yR7s). Their primary synaptic targets, Dm8 amacrine neurons, express DIP-γ. In dpr11 or DIP-γ mutants, yR7 terminals extend beyond their normal termination zones in layer M6 of the medulla. DIP-γ is also required for Dm8 survival or differentiation. Our findings suggest that Dpr-DIP interactions are important determinants of synaptic connectivity.

PubMed: 26687361
DOI: 10.1016/j.cell.2015.11.022

実験手法

X-RAY DIFFRACTION (2.2988 Å)