FIGURE

Figure 6

ID
ZDB-FIG-210719-6
Publication
Adams et al., 2021 - A two-site flexible clamp mechanism for RET-GDNF-GFRα1 assembly reveals both conformational adaptation and strict geometric spacing
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Figure 6

Divergent GFRα1/GFRAL co-receptor D1 domain positions within the RETECD ternary complex

(A) The D1-D2 domain linker motif (SPYE), highlighted in cyan is conserved between zGFRα1a, GFRα1, GFRα2, and GFRα3. It is missing from the shorter GFRα4 that lacks a D1 domain altogether and from the divergent GFRAL.

(B) Schematic diagram of human RETECD, GFRAL, and GDF15 construct boundaries used and individual domains annotated as in Figure 1.

(C) (i) Negative stain EM envelope of a reconstituted hRETECD2-hGDF152-hGFRAL2 (hR15AL) complex docked with hR15AL (PDB: 6Q2J) revealing additional map potential indicated by a green Gaussian volume (generated from a D1 domain homology model). (ii) Cryo-EM map of zRGα1a (light gray) superposed with the final model (colored as in Figure 2) with GFRα1aD1 shown (light green Gaussian volume at 5 Å2).

(D) Comparison of co-receptor D1 domain position and interfaces (i) GFRALD1 makes different contacts to domains D2-D3 (green), GFRALD1 shown as a 30 Å2 Gaussian volume (light green), and GDF15 (salmon). (ii) zGFRα1aD1 contacts and colored as in Figure 2. zGFRα1aD1 represented as a 5 Å2 Gaussian volume (light green).

Expression Data

Expression Detail
Antibody Labeling
Phenotype Data

Phenotype Detail
Acknowledgments
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Reprinted from Structure (London, England : 1993), 29(7), Adams, S.E., Purkiss, A.G., Knowles, P.P., Nans, A., Briggs, D.C., Borg, A., Earl, C.P., Goodman, K.M., Nawrotek, A., Borg, A.J., McIntosh, P.B., Houghton, F.M., Kjær, S., McDonald, N.Q., A two-site flexible clamp mechanism for RET-GDNF-GFRα1 assembly reveals both conformational adaptation and strict geometric spacing, 694-708.e7, Copyright (2021) with permission from Elsevier. Full text @ Structure