HIV Protease Hinge Region Insertions at Codon 38 Affect Enzyme Kinetics, Conformational Stability and Dynamics.

ABSTRACT: HIV-1 protease is essential for the production of mature, infectious virions and is a major target in antiretroviral therapy. We successfully purified a HIV-1 subtype C variant, L38↑N↑L^- 4, containing an insertion of asparagine and leucine at position 38 without the four background mutations - K20R, E35D, R57K, V82I using a modified purification protocol. Isothermal titration calorimetry indicated that 50% of the variant protease sample was in the active conformation compared to 62% of the wild type protease. The secondary structure composition of the variant protease was unaffected by the double insertion. The specific activity and k_cat values of the variant protease were approximately 50% lower than the wild type protease values. The variant protease also exhibited

SUBMITTER: Sheik Ismail Z 

PROVIDER: S-EPMC10480237 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature