Characterizing the protonation states of the catalytic residues in apo and substrate-bound human T-cell leukemia virus type 1 protease
Protonation states of the catalytic residues in HTLV-1 protease were investigated. In apo HTLV-1 protease, the two catalytic residues are both unprotonated. In HTLV-1 proteasesubstrate complex, Asp32 is protonated, Asp32? is unprotonated. Substrate binding favors a protonated Asp32 over protonated Asp32? by 2.8kcal/mol. The HTLV-1 proteasesubstrate complex structure was analyzed in detail.
protonation states catalytic residues htlv-1 protease free energy simulations qm/mm