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. Author manuscript; available in PMC: 2013 May 10.
Published in final edited form as: Virology. 2012 Feb 23;426(2):188–196. doi: 10.1016/j.virol.2012.01.034

Figure 2. IN constructs and sequence alignments.

Figure 2

(A) Sequence alignment of MuLV, PFV, and HIV-1 CTDs. Secondary structural elements are shown above where E denotes residues in a beta conformation and H denotes residues in a helical conformation (β, beta strands; η, 310 helix). Asterisk denotes K376 in MuLV and the homologous lysine residues in PFV and HIV-1 reported. Amino acid numbering corresponds to MuLV IN. The MuLV CTD was structurally aligned (P. Rossi, personal communication) to PFV and HIV-1 CTDs with UCSF Chimera (Pettersen et al., 2004). (B) Diagram depicts the three domains of IN: Zn+ binding NTD, CCD, and CTD with residues of interest highlighted. Grey line in the NTD denotes the additional 50 amino acids in MLV IN not present in HIV IN. Grey line in CTD marks the non-essential extreme C-terminal 23 amino acids.

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