Extended Data Fig. 7: Comparison of surface representation of BRCT domains of Rev1 with PARP1, RFC, and BRCA1. | Nature Structural & Molecular Biology

Extended Data Fig. 7: Comparison of surface representation of BRCT domains of Rev1 with PARP1, RFC, and BRCA1.

From: Cryo-EM structure of the Rev1–Polζ holocomplex reveals the mechanism of their cooperativity in translesion DNA synthesis

Extended Data Fig. 7: Comparison of surface representation of BRCT domains of Rev1 with PARP1, RFC, and BRCA1.

a, Structural alignment of the BRCT domains of Rev1, PARP1, RFC and BRCA1. b, Electrostatic surface potential of the Rev1 N-helix-BRCT module shows an extensive positively charged surface (blue) for binding DNA (red). c, d, Electrostatic surface potentials of the PARP1 (c) and RFC BRCT (d) domains are also positively charged (blue) for interacting with DNA (red) e, Electrostatic surface potential of the BRCA1 BRCT1 differs from that of Rev1/PARP1/RFC BRCT domains.

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