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. 2007 Jan 31;81(8):3807–3815. doi: 10.1128/JVI.02795-06

FIG. 1.

FIG. 1.

(A) Structure model of the N-terminal CDA domain of A3G. Zinc-coordinating residues are indicated by circles, α-helices are in yellow, and β-strands are in pink. The position of residue D128 is indicated in the predicted loop between β4 and α3. (B) The amino acid sequence of residues 114 to 153 of A3G. The positions of predicted α-helix (yellow) and β-strand (pink) regions are indicated, as are residues 119, 128, and 146. The motifs defined here as being important for HIV-1 packaging and Vif responsiveness are indicated.