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. 2019 Aug 8;75(3):483–497.e9. doi: 10.1016/j.molcel.2019.06.002

Figure 3.

Figure 3

RAP80 Controls BRE Conformation and Prevents Dimerization

(A) A fusion scaffold protein containing residues 1–260 of mouse ABRO1 fused to residues 269–407 of mouse ABRAXAS disrupts dimerization (native PAGE) and integrates RAP80 stoichiometrically into the complex (SDS-PAGE).

(B) The structure of BRISC dimer. A pseudoatomic model of BRISC was generated by rigid-body fitting of the atomic BRISC model derived from the cryo-EM structure determination of BRISC-SHMT2α complex into the density map of BRISC dimer.

(C) Integration of RAP80 into BRCA1-A results in a substantial conformation change of BRE as evidenced by a comparison of the structures of BRCA1-A and BRISC.