P2-binding site on TCS was mapped to the C-terminal domain by chemical shift perturbation

Abstract

<p><b>Copyright information:</b></p><p>Taken from "Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses"</p><p></p><p>Nucleic Acids Research 2007;35(5):1660-1672.</p><p>Published online 18 Feb 2007</p><p>PMCID:PMC1865052.</p><p>© 2007 The Author(s).</p> () H–N correlation spectra of TCS in the absence (black contours) and in the presence (red contours) of equal molar ratio of P2 were compared, and () changes in chemical shifts, ▵ppm(HN) and ▵ppm(N), of amide resonances of TCS were measured. Residues with ▵ppm(HN) >0.075 ppm or ▵ppm(N) >0.5 ppm are indicated in (a) and (b), and colour-coded magenta in the stereo diagram of TCS in (). These residues are localized in or near the C-terminal domain (173–247, colour-coded green) of TCS. Scanning alanine mutagenesis was performed on all charge residues in the C-terminal domain and E123, which are indicated in (c)