Fig 2.

Protein folding of RING domain mutants. (A) Structure of the RING domain of TRIM5α_rh illustrating the position of tyrosine 63 (red). The side chain of tyrosine 63 is part of the hydrophobic core of the RING domain and is surrounded by the hydrophobic side chains of residues L28, I39, I61, P65, and I68. (B) The two-dimensional ¹H, ¹⁵NHSQC spectra of wild-type (black) and Y63E (red) RING domains are shown. The overlay of the spectral data (black and red) showed that the RING domain Y63E mutation does not disrupt protein folding.