Understanding HTLV-I Protease

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Understanding HTLV-I Protease Suzanne Beckham Shuker, Victoria L. Mariani, Bryan E. Herger, Kelly J. Dennison Chemistry & Biology Volume 10, Issue 5, Pages 373-380 (May 2003) DOI: 10.1016/S1074-5521(03)00104-2

Figure 1 Structure of HIV-1 Protease One monomer is colored blue and the other is colored magenta. The catalytic aspartic acids are highlighted in green. Chemistry & Biology 2003 10, 373-380DOI: (10.1016/S1074-5521(03)00104-2)

Figure 2 Sequence Alignment of the Leukemia Retrovirus Proteases with Retroviral Proteases of Known Structure The alignment for HIV-1, HIV-2, SIV, FIV, EIAV, and RSV proteases was generated based on the reported structures (PDB IDs: HIV-1, 1A30; HIV-2, 1HSI; SIV, 1YTH; FIV, 1B11; EIAV, 1FMB; and RSV, 1BAI). These structures have the following mutations from the wild-type proteases: HIV-1: Q7K, L33I, L63I; SIV: Q7K; EAIV: I54G; RSV: S38T, I42D, I44V, M73V, A100L, V104T, R105P, G106V, and S107N. Hydrophobic residues are indicated in yellow, hydrophilic residues in green, acidic residues in red, and basic residues in blue. Abbreviations: BLV, bovine leukemia virus; MuLV, murine leukemia virus; SIV, simian immunodeficiency virus; FIV, feline immunodeficiency virus; EIAV, equine infectious anemia virus; RSV, Rous sarcoma virus. Chemistry & Biology 2003 10, 373-380DOI: (10.1016/S1074-5521(03)00104-2)

Figure 3 Homology Model of HTLV-I Protease without the Ten C-Terminal Residues The subsites are shown in spacefilling representation (S4 and S4′, top left; S3 and S3′, top right; S2 and S2′, bottom left; S1 and S1′, bottom right) with hydrophobic residues colored in green and hydrophilic residues colored by element. The catalytic aspartic acids are shown in purple and the substrate is shown in orange. PDB ID of HTLV-I protease is 1O0J. Chemistry & Biology 2003 10, 373-380DOI: (10.1016/S1074-5521(03)00104-2)