Figure 2: PrimPol possesses a second RBM that also binds to the basic cleft of RPA70N. | Nature Communications

Figure 2: PrimPol possesses a second RBM that also binds to the basic cleft of RPA70N.

From: Molecular basis for PrimPol recruitment to replication forks by RPA

Figure 2

(a) The sequence of PrimPol’s RBM-B (residues 542–560), located in the C-terminal RBD (residues 480–560). (b) The continuous electron density of RBM-B residues 548–556 in the complex with RPA70N. (c) Electrostatic surface model of RPA70N with RBM-B (green) bound in the basic cleft. Basic and acidic surfaces are coloured blue and red, respectively. (d) 15N-1H HSQC spectra showing RPA70N in the absence (black) or presence (red) of a twofold molar excess of unlabelled RBM-B peptide. (e) Key stabilizing interactions of RBM-B (green) in the RPA70N basic cleft (purple). RBM-B binds between β sheets in the β barrel of RPA70N. D551 is of particular importance as it forms a number of electrostatic interactions with both the side chains and a backbone amide NH of the RPA70N peptide.

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