Figure 2 Identification of the binding site for Rpn10[196 -306]
in the parkin ubiquitin-like (Ubl) domain. (A) 1H-15N
heteronuclear single-quantum coherence (HSQC) spectrum of the
parkin Ubl domain in the presence (red) and absence (black) of
equimolar quantities of Rpn10[196 -306]. The peaks labelled with
L-2, G-1 and S0 originate from the amino-terminal tag. (B) NMR
chemical-shift-perturbation data for the parkin Ubl domain. The
data are displayed for each residue according to the equation
represent the change in nitrogen and proton chemical shifts on
addition of Rpn10[196 -306]. Asterisks indicate residues the
peaks of which became undetectable due to broadening. Secondary
structure elements for the parkin Ubl are shown below the graph.
(C) Mapping of the perturbed residues of the Ubl domains of
parkin and PLIC2 (Walters et al., 2002) on binding to Rpn10.
Residues showing a chemical-shift-perturbation are coloured in
red, with the colour gradient indicating the strength of the
perturbation. Residues the peaks of which became undetectable on
binding to Rpn10 are shown in purple.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd: