FIGURE

Figure 1

ID

ZDB-FIG-210719-1

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 1

Crystal structure and flexibility of the zRET CLD(1-4) module

(A) Schematic of zebrafish RET receptor tyrosine kinase. CLD, cadherin-like domains; CRD, cysteine-rich domain; TM, transmembrane helix; JM, juxtamembrane domain; KD, kinase domain.

(B) Orthogonal views of zRET^CLD1-4 colored as in (A). The calcium-binding site between CLD(2-3) has three calcium ions as green spheres with coordinating ligands as sticks and waters as red spheres.

(D) Close-up of the interface between CLD3 and CLD4 centered on R272, selected side chains shown as sticks and dashed lines for hydrogen bonds.

(E) Superposition of chains A and B within the crystallographic asymmetric unit.

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