Fig. 3: rA3G CD1-CD2 domain arrangement and the conserved core structure of rA3G binding to the AA dinucleotides.
From: Structural basis of sequence-specific RNA recognition by the antiviral factor APOBEC3G
a Superimposition of the CD1 of the RNA-bound rA3G structure and two apo-rA3G structures, showing the CD2 turns ~135° and rotates about 180° from the CD2 of apo-rA3G. b The interface between CD1 and CD2 in the RNA-bound rA3GR8/E259A structure (PDB ID: 7UU4). The interface residues with a buried surface area larger than 10 Å2 are shown. See Supplementary Fig. 5 for the detailed arrangement of the interface residues. c The surface electrostatic potential of rA3GR8/E259A with superimposition of the three bound RNA molecules. The conserved core-binding structure of the sequence motif 5′-(U/G)AA-3′ (inside a white dotted circle) is indicated. The two structural features on the rA3GR8/E259A surface, the pocket and the groove, are indicated. The electrostatic surface potential is colored from red to blue with −5 to +5 kT/e. The molecules in panels b and c are positioned similarly.
