Comparison of inhibitor binding in HIV‐1 protease and in non‐viral aspartic proteases: the role of the flap

FEBS Letters

Weber, Irene T.¹  Gustchina, Alla¹ 

[1] Crystallography Laboratory, NCI-Frederick Cancer Research and Development Center, ABL-Basic Research Program, Frederick, MD 21701, U.S.A.

关键词: Retroviral protease;    Aspartic protease;    Enzyme-substrate interaction;    Retroviral polyprotein precursor;   

DOI  :  10.1016/0014-5793(90)81171-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structure of HIV-1 protease with an inhibitor has been compared with the structures of non-viral aspartic proteases complexed with inhibitors. In the dimeric HIV-1 protease, two 4-stranded β-sheets are formed by half of the inhibitor, residues 27–29, and the flap from each monomer. In the monomeric non-viral enzyme the single flap does not form a β-sheet with an inhibitor. The HIV-1 protease shows more interactions with a longer peptide inhibitor than are observed in non-viral aspartic protease-inhibitor complexes. This, and the large movement of the flaps, restricts the conformation of the protease cleavage sites in the retroviral polyprotein precursor.

【 授权许可】

Unknown