6NRX

Crystal structure of DIP-eta IG1 homodimer

6NRX の概要

• エントリーDOI: 10.2210/pdb6nrx/pdb
• 関連するPDBエントリー: 5EO9 6NRQ 6NRR 6NRW
• 分子名称: Dpr-interacting protein eta, isoform B, 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: immunoglobulin superfamily, glycoprotein, neuronal, cell surface receptor, cell adhesion
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26508.46

構造登録者

Cheng, S.,Park, Y.J.,Kurleto, J.D.,Ozkan, E. (登録日: 2019-01-24, 公開日: 2019-02-06, 最終更新日: 2024-10-09)

主引用文献

Cheng, S.,Ashley, J.,Kurleto, J.D.,Lobb-Rabe, M.,Park, Y.J.,Carrillo, R.A.,Ozkan, E.
Molecular basis of synaptic specificity by immunoglobulin superfamily receptors in Drosophila.
Elife, 8:-, 2019

PubMed Abstract: In stereotyped neuronal networks, synaptic connectivity is dictated by cell surface proteins, which assign unique identities to neurons, and physically mediate axon guidance and synapse targeting. We recently identified two groups of immunoglobulin superfamily proteins in , Dprs and DIPs, as strong candidates for synapse targeting functions. Here, we uncover the molecular basis of specificity in Dpr-DIP mediated cellular adhesions and neuronal connectivity. First, we present five crystal structures of Dpr-DIP and DIP-DIP complexes, highlighting the evolutionary and structural origins of diversification in Dpr and DIP proteins and their interactions. We further show that structures can be used to rationally engineer receptors with novel specificities or modified affinities, which can be used to study specific circuits that require Dpr-DIP interactions to help establish connectivity. We investigate one pair, engineered Dpr10 and DIP-α, for function in the neuromuscular circuit in flies, and reveal roles for homophilic and heterophilic binding in wiring.

PubMed: 30688651
DOI: 10.7554/eLife.41028

実験手法

X-RAY DIFFRACTION (1.9 Å)