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. 2010 Apr 20;285(26):20303–20315. doi: 10.1074/jbc.M110.114413

FIGURE 1.

FIGURE 1.

A, IN and LEDGF/p75 proteins. IN is composed of three structural domains as follows: an N-terminal domain (green), a catalytic core domain (red), and a C-terminal domain (yellow). The integrase binding domain of LEDGF/p75 is shown in magenta. B, representative data for sedimentation equilibrium analysis of IN(tetra)·LEDGF(IBD). Global fits were performed at three concentrations at three rotor speeds. Top panels are radial absorbance data (symbols) and model fits (lines). Bottom panels are residuals from the fits. Experiments were carried out at 12,000, 16,000, and 20,000 rpm. C, representative SEC-MALS analyses of IN·LEDGF complexes. The top panel shows the elution profile of IN(tetra)·LEDGF(IBD) (red line) from a TSK3000 analytical column. The middle panel and lower panels show the elution profiles for wild-type IN·LEDGF(Cterm) (green) and IN(tetra)(D116N)·LEDGF(Cterm) (cyan) from a TSK4000 column. Wild-type IN preparations showed evidence of higher order species that are greatly reduced in IN(tetra) preparations. D, representative sedimentation velocity analyses. c(S) distributions for IN(tetra)·LEDGF(IBD) (red line, top panel), IN·LEDGF(Cterm) (green, middle panel), and IN(tetra)·LEDGF(Cterm) (cyan, lower panel) are shown.