Crystallization (Comment) | Organism |
---|---|
determination of the crystal structures of three chimeric HIV proteases complexed with SB203386. The chimeras are constructed by substituting amino acid residues in the HIV type 1 protease sequence with the corresponding residues from HIV type 2 in the region spanning residues 31-37 and in the active site cavity. Crystallographic analysis reveals that substitution of residues 31-37 (30's loop) with those of HIV-2 protease renders the chimera similar to HIV-2 protease in both the inhibitor binding affinity and mode of binding (two inhibitor molecules per protease dimer). However, further substitution of active site residues 47 and 82 has a compensatory effect which restores the HIV-1-like inhibitor binding mode | Human immunodeficiency virus 1 |
Protein Variants | Comment | Organism |
---|---|---|
additional information | three chimeric HIV proteases are constructed by substituting amino acid residues in the HIV type 1 protease sequence with the corresponding residues from HIV type 2 in the region spanning residues 31-37 and in the active site cavity. Crystallographic analysis reveals that substitution of residues 31-37 (30's loop) with those of HIV-2 protease renders the chimera similar to HIV-2 protease in both the inhibitor binding affinity and mode of binding (two inhibitor molecules per protease dimer). However, further substitution of active site residues 47 and 82 has a compensatory effect which restores the HIV-1-like inhibitor binding mode | Human immunodeficiency virus 1 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
SB203386 | - |
Human immunodeficiency virus 1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 1 | - |
- |
- |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000018 | - |
SB203386 | - |
Human immunodeficiency virus 1 |