5eo9

Crystal Structure of the complex of Dpr6 Domain 1 bound to DIP-alpha Domain 1+2

spinqualitylabelsall models 5eo9, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5eo9 is a 2 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 2.2988Å Ligands: NAG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M9PC40_DROME Publication Abstract from PubMed We have defined a network of interacting Drosophila cell surface proteins in which a 21-member IgSF subfamily, the Dprs, binds to a nine-member subfamily, the DIPs. The structural basis of the Dpr-DIP interaction code appears to be dictated by shape complementarity within the Dpr-DIP binding interface. Each of the six dpr and DIP genes examined here is expressed by a unique subset of larval and pupal neurons. In the neuromuscular system, interactions between Dpr11 and DIP-gamma affect presynaptic terminal development, trophic factor responses, and neurotransmission. In the visual system, dpr11 is selectively expressed by R7 photoreceptors that use Rh4 opsin (yR7s). Their primary synaptic targets, Dm8 amacrine neurons, express DIP-gamma. In dpr11 or DIP-gamma mutants, yR7 terminals extend beyond their normal termination zones in layer M6 of the medulla. DIP-gamma is also required for Dm8 survival or differentiation. Our findings suggest that Dpr-DIP interactions are important determinants of synaptic connectivity. Control of Synaptic Connectivity by a Network of Drosophila IgSF Cell Surface Proteins.,Carrillo RA, Ozkan E, Menon KP, Nagarkar-Jaiswal S, Lee PT, Jeon M, Birnbaum ME, Bellen HJ, Garcia KC, Zinn K Cell. 2015 Dec 17;163(7):1770-82. doi: 10.1016/j.cell.2015.11.022. PMID:26687361 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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