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6EG0

Crystal structure of Dpr4 Ig1-Ig2 in complex with DIP-Eta Ig1-Ig3

Summary for 6EG0
Entry DOI10.2210/pdb6eg0/pdb
DescriptorDefective proboscis extension response 4, ACETATE ION, Dpr-interacting protein eta, isoform B, ... (11 entities in total)
Functional Keywordsimmunoglobulin super-family, synaptic specification, nervous system development, cell-surface protein, cell adhesion
Biological sourceDrosophila melanogaster (Fruit fly)
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Total number of polymer chains2
Total formula weight63999.72
Authors
Cosmanescu, F.,Shapiro, L. (deposition date: 2018-08-17, release date: 2018-11-28, Last modification date: 2024-11-20)
Primary citationCosmanescu, F.,Katsamba, P.S.,Sergeeva, A.P.,Ahlsen, G.,Patel, S.D.,Brewer, J.J.,Tan, L.,Xu, S.,Xiao, Q.,Nagarkar-Jaiswal, S.,Nern, A.,Bellen, H.J.,Zipursky, S.L.,Honig, B.,Shapiro, L.
Neuron-Subtype-Specific Expression, Interaction Affinities, and Specificity Determinants of DIP/Dpr Cell Recognition Proteins.
Neuron, 100:1385-, 2018
Cited by
PubMed Abstract: Binding between DIP and Dpr neuronal recognition proteins has been proposed to regulate synaptic connections between lamina and medulla neurons in the Drosophila visual system. Each lamina neuron was previously shown to express many Dprs. Here, we demonstrate, by contrast, that their synaptic partners typically express one or two DIPs, with binding specificities matched to the lamina neuron-expressed Dprs. A deeper understanding of the molecular logic of DIP/Dpr interaction requires quantitative studies on the properties of these proteins. We thus generated a quantitative affinity-based DIP/Dpr interactome for all DIP/Dpr protein family members. This revealed a broad range of affinities and identified homophilic binding for some DIPs and some Dprs. These data, along with full-length ectodomain DIP/Dpr and DIP/DIP crystal structures, led to the identification of molecular determinants of DIP/Dpr specificity. This structural knowledge, along with a comprehensive set of quantitative binding affinities, provides new tools for functional studies in vivo.
PubMed: 30467080
DOI: 10.1016/j.neuron.2018.10.046
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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