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Figure 2
Alignment of retroviral proteases. (a) Stereoview of the superposition of the Cα traces of protomers of retroviral proteases: green and blue, M-PMV (A and B); red, HIV-1, apo form (PDB entry 3hvp ); orange, HIV-1, inhibitor complex (PDB entry 4hvp ); lime, EIAV (PDB entry 2fmb ); grey, M-PMV, NMR model (PDB entry 1nso ), energy-minimized (in water). (b) Structure-based sequence alignment of the M-PMV, EIAV (PDB entry 2fmb ; lowest core Cα r.m.s.d.; Table 2[link]), FIV (PDB entry 4fiv ; highest level of sequence identity – 26.6%) and HIV-1 (PDB entry 3hvp ) proteases. Residue numbers and secondary-structure elements (arrows, β-strands; blue, α-helices; green, 310-helices; yellow, flap loops) are marked for the M-­PMV and HIV-1 proteases. Residues that are identical in all four sequences are shown on a red background. Disordered residues missing from the M-PMV PR structure are shown in grey.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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