Radixin

spinqualitylabelsall models Mouse radixin FERM domain (green) complex with N-terminal peptide of the adhesion molecule PSGL-1 (yellow) (PDB code 2emt) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Radixin (Rdx) plays an important role in promoting cell migration by regulating Rac-1-mediated epithelial polarity and formation of adherens junctions through Rac guanine nucleotide exchange factors. Rdx is part of the ERM (Ezrin/Radixin/Moesin) which is linked to cell shape change. Phosphorylation of the C-terminal Thr residues of ERM inhibits cell adhesion and induces formation of spherical cell shape. Disease Rdx deficiency causes increase in bilirubin in serum, a phenotype similar to that of Dubin-Johnson syndrome in human. Structural highlights The hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule P-selectin glycoprotein ligand 1 with multiple hydrogen bonds. Hydrophobic, Polar

3D Structures of radixin

Updated on 25-August-2019

1gc7, 2d2q – mRdx FERM domain – mouse
3x23, 2ems, 2yvc, 2d10, 2d11, 2emt, 1j19, 2zpy – mRdx FERM domain + peptide
1gc6 – mRdx FERM domain + inositol-triphosphate

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Michal Harel, Alexander Berchansky, Joel L. Sussman