6NRX

Crystal structure of DIP-eta IG1 homodimer

Summary for 6NRX

• Entry DOI: 10.2210/pdb6nrx/pdb
• Related: 5EO9 6NRQ 6NRR 6NRW
• Descriptor: Dpr-interacting protein eta, isoform B, 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (4 entities in total)
• Functional Keywords: immunoglobulin superfamily, glycoprotein, neuronal, cell surface receptor, cell adhesion
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 2
• Total formula weight: 26508.46

Authors

Cheng, S.,Park, Y.J.,Kurleto, J.D.,Ozkan, E. (deposition date: 2019-01-24, release date: 2019-02-06, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)