A model of the three-dimensional structure of human endogenous retrovirus protease
Pechik, I.V.; Andreeva, N.S.
Molekuliarnaia Biologiia 33(6): 1035-1042
1999
ISSN/ISBN: 0026-8984 PMID: 10624695 Document Number: 510756
Aspartate protease of endogenous human virus HERV-K plays the key role in its vital cycle. Besides its main function of processing HERV-K polyprotein, this protease is also able to process HIV-1 polyprotein. A model of the spatial structure of HERV-K protease based on the homologies to the structures of some virus aspartate proteases was designed to analyze the structural principles of its specificity. The model was compared to the structure (determined by x-rays) of the complex of HIV-1 protease and inhibitor. Special attention was paid to the similarity of binding pockets and differences between them. Amino acid residues responsible for binding specificity were identified. An attempt was made to give a structural explanation of the resistance of HERV-K protease to HIV-1 protease inhibitors.