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. Author manuscript; available in PMC: 2020 Aug 22.
Published in final edited form as: Mol Cell. 2019 Jul 9;75(4):781–790.e3. doi: 10.1016/j.molcel.2019.06.007

Figure 3. Conformational changes in the α5 helix and its surrounding regions upon Rho engagement.

Figure 3.

Comparison of Ras domain structural elements in GT·GDP and Rho-GT-Nb35*. (A) GαT in GT·GDP (PDB: 1GOT, grey). Residues 344-LKDCGLF-350 at the C terminus are shown as a dashed curve as they are not resolved in the GT·GDP crystal structure. The helical domain is shown as a transparent cartoon for reference. (B) eGαT in the Rho-GT-Nb35* complex (lime) aligned to GT·GDP based on Gβ1γ1.

See also Figures S3 and S5.