Crystallization (Comment) | Organism |
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all-atom molecular dynamics simulations for both retroviral proteases from HIV-1 and HTLV-I in their ligand-free states and in complex with model substrates. The two catalytic aspartates D32/D32' of HTLV-PR exhibit slightly repulsive interactions with the substrate. Inspection of the electrostatic interaction energy, reveals a large attractive electrostatic interaction of D32/D32' with the substrate that overcompensates for the repulsive van der Waals interactions. The nonconserved residues HIV-PR D30/D30' and HTLV-PR M37/M37' also contribute strongly to the binding of the substrate analogs in both proteases. Interactions in both proteases occur at the same spatial sites and with similar binding energies. There care high similarities between the dynamic behaviors of the flap structures, especially in the ligand-free state | Human T-cell leukemia virus type I |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human T-cell leukemia virus type I | P03362 | Gag-Pro-Pol-polyprotein including protease | - |
Human T-cell leukemia virus type I Japan ATK-1 subtype A | P03362 | Gag-Pro-Pol-polyprotein including protease | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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Ac-Ala-Pro-Gln-Val-Sta-Val-Met-His-Pro | substrate analogue, based on the natural MA/CA cleavage site of HTLV-I protease | Human T-cell leukemia virus type I | ? | - |
? | |
Ac-Ala-Pro-Gln-Val-Sta-Val-Met-His-Pro | substrate analogue, based on the natural MA/CA cleavage site of HTLV-I protease | Human T-cell leukemia virus type I Japan ATK-1 subtype A | ? | - |
? |