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. 2010 Feb 24;285(18):13599–13606. doi: 10.1074/jbc.M109.089540

FIGURE 2.

FIGURE 2.

Solution studies of PABPC1 Mlle binding the GW182 DUF region. a, ITC trace (top) and integrated areas (bottom) for GW182-(1380–1401) binding to the PABPC1 Mlle domain. b, backbone amide 15N{1H} heteronuclear nuclear Overhauser effects for 15N-labeled GW182 peptide bound to Mlle domain. Values above 0.6 indicate highly ordered residues. c, chemical shift changes in the 15N-labeled PABPC1 Mlle domain (residues 544–626) upon addition of a peptide comprising the GW182 DUF region. Shifts are calculated as a weighted average in ppm as (ΔH2 + (ΔN/5)2)1/2. d, mapping of the chemical shift changes by residue color (white, no change; black, maximum change) onto a schematic representation of the unliganded Mlle domain. For reference, the position of the GW182 peptide in the x-ray crystal structure is shown.