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Literature summary for 3.4.23.B8 extracted from

  • Rücker, P.; Horn, A.; Meiselbach, H.; Sticht, H.
    A comparative study of HIV-1 and HTLV-I protease structure and dynamics reveals a conserved residue interaction network (2011), J. Mol. Model., 17, 2693-2705.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Human T-cell leukemia virus type I P03362 Gag-Pro-Pol-polyprotein including protease
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Human T-cell leukemia virus type I Japan ATK-1 subtype A P03362 Gag-Pro-Pol-polyprotein including protease
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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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 Japan ATK-1 subtype A ?
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