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. 2010 Dec 27;108(2):534–539. doi: 10.1073/pnas.1013426108

Fig. 3.

Fig. 3.

TRIM5-21R binding to helical tubes of cysteine-crosslinked HIV-1 CA hexamers requires the SPRY domain and is enhanced by B-box 2 domain interactions. TRIM5-21R proteins were incubated in the absence of CA (lanes 1–3 and 7–9) or in the presence of a 6-fold molar excess of CA subunits assembled into helical tubes that mimic the hexagonal capsid lattice (lanes 4–6 and 10–12). Binding experiments were performed at two different TRIM5-21R protein concentrations (0.5 μM, lanes 1–6 or 1 μM, lanes 7–12) using either wild-type, full-length TRIM5-21R proteins (WT, lanes 1, 4, 7, and 10), TRIM5-21R proteins with the R121E mutation (R121E, lanes 2, 5, 8, and 11), or truncated TRIM5-21R proteins that lacked the SPRY domain (ΔSPRY, lanes 3, 6, 9, and 12). Pelletable CA and associated TRIM5-21R proteins (Pellet, 4% of total), were separated from unassembled and soluble CA proteins and unbound TRIM5-21R (Supernatant, 1% of total) by centrifugation, and analyzed by Western blotting, with the input levels of both proteins shown for reference (Input, 1% of total).