6ns1

Crystal structure of DIP-gamma IG1+IG2Crystal structure of DIP-gamma IG1+IG2

Structural highlights 6ns1 is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9VAR6_DROME Publication Abstract from PubMed 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 Drosophila, 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-alpha, for function in the neuromuscular circuit in flies, and reveal roles for homophilic and heterophilic binding in wiring. Molecular basis of synaptic specificity by immunoglobulin superfamily receptors in Drosophila.,Cheng S, Ashley J, Kurleto JD, Lobb-Rabe M, Park YJ, Carrillo RA, Ozkan E Elife. 2019 Jan 28;8. pii: 41028. doi: 10.7554/eLife.41028. PMID:30688651 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6ns1, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image