Fig. 1: Crystallographic evidence for a decameric assembly of zGDNF-zGFRα1D2-D3. | Nature Communications

Fig. 1: Crystallographic evidence for a decameric assembly of zGDNF-zGFRα1D2-D3.

From: Architecture and regulation of a GDNF-GFRα1 synaptic adhesion assembly

Fig. 1

a Domain organisation for zGFRα1D2-D3 and zGDNFmat with discrete colours for individual domains. b Orthogonal views of the zGFRα1D2-D3-zGDNFmat assembly crystal structure. Domains are coloured according to (a), zGFRα1-D2, light green, zGFRα1-D3 dark green, GDNF dimer protomers yellow and orange. N-glycans attached to zGDNF and zGFRα1-D3 are shown as sticks. Bottom view projects directly down the five-fold rotational symmetry axis. c zGFRα1 interface between each subunit of the pentameric ring, opened to highlight secondary structure elements and interacting residues at the site of contact. Main chain atoms are shown as a cartoon and interaction residues as sticks. A transparent surface (green) and interaction surface (purple) are also shown. d Close up view of the zGFRα1 pentameric interface with key interacting residues shown as sticks with hydrogen-bonds displayed as dashed lines. e Schematic model for zGDNFmat zGFRα1D2-D3 decameric complex assembly in vitro. The model emphasises a 2:2 zGDNFmat-zGFRα1D2-D3 complex intermediate that multimerises through GFRα1 homophilic interactions.

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