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6NRW

Crystal structure of Dpr1 IG1 bound to DIP-eta IG1

Summary for 6NRW
Entry DOI10.2210/pdb6nrw/pdb
Related5EO9 6NRQ 6NRR
DescriptorDPR1, Dpr-interacting protein eta, isoform B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
Functional Keywordsimmunoglobulin superfamily, glycoprotein, neuronal, cell surface receptor, cell adhesion
Biological sourceDrosophila melanogaster (Fruit fly)
More
Total number of polymer chains4
Total formula weight55313.20
Authors
Cheng, S.,Park, Y.J.,Kurleto, J.D.,Ozkan, E. (deposition date: 2019-01-24, release date: 2019-02-06, Last modification date: 2023-10-11)
Primary citationCheng, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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数据于2024-11-06公开中

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