Figure 3From: What does the structure-function relationship of the HIV-1 Tat protein teach us about developing an AIDS vaccine?NMR studies of Tat proteins. Tat Z2 (A), Tat Bru (B), Tat Mal (C), and Tat Eli (D) 3D structures obtained from NMR constraints [36–38, 44]. Region I is depicted in red, region II (cysteine-rich region) in orange, region III in yellow, region IV (basic region) in green, region V in light blue, region VI (residues 73–86/87) in blue and for Tat Eli the extra C-terminal residues are in pink. The Tat Z2 variant used had chemically modified cysteines which affected biological activity and 3D structure. The three Tat variants with biological activity (B, C and D) displayed a similar folding characterized by a core region composed of part of region I with the highly conserved Trp11 while the functional region II, IV and V are well exposed to the solvent. The extra residues in the C-terminus of Tat Eli are exposed to the solvent and protrude from a groove between the basic region and the cysteine-rich region.Back to article page