Open access
Aug 2026
Structure and enzymatic properties of human retroviral-like aspartic protease 1 and functional roles of disease-associated mutations.
Structural analysis reveals that ASPRV1-14 possesses distinctly hydrophobic S2/S2' pockets, dictating a strict requirement for hydrophobic residues at the P2/P2' positions of substrates and explaining its resistance to most HIV-1 PR inhibitors, except indinavir.
Xueqian Feng, Zi-Lian Chen, Chao Lan et al.
· Acta Biochimica et Biophysic... · 0 citations