Molecular modeling of the HIV-1 protease and its substrate binding site

Irene T. Weber; Maria Miller; Mariusz Jaskólski; Jonathan Leis; Anna Marie Skalka; Alexander Wlodawer

doi:10.1126/science.2537531

Molecular modeling of the HIV-1 protease and its substrate binding site

Irene T. Weber^*, Maria Miller, Mariusz Jaskólski, Jonathan Leis, Anna Marie Skalka, Alexander Wlodawer

^*Corresponding author for this work

Microbiology-Immunology

Research output: Contribution to journal › Article › peer-review

152 Scopus citations

Abstract

The human immunodeficiency virus (HIV-1) encodes a protease that is essential for viral replication and is a member of the aspartic protease family. The recently determined three-dimensional structure of the related protease from Rous sarcoma virus has been used to model the smaller HIV-1 dimer. The active site has been analyzed by comparison to the structure of the aspartic protease, rhizopuspepsin, complexed with a peptide inhibitor. The HIV-1 protease is predicted to interact with seven residues ofthe protein substrate. This information can be used to design protease inhibitors and possible antivirual drugs.

Original language	English (US)
Pages (from-to)	928-931
Number of pages	4
Journal	Science
Volume	243
Issue number	4893
DOIs	https://doi.org/10.1126/science.2537531
State	Published - 1989

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abstract = "The human immunodeficiency virus (HIV-1) encodes a protease that is essential for viral replication and is a member of the aspartic protease family. The recently determined three-dimensional structure of the related protease from Rous sarcoma virus has been used to model the smaller HIV-1 dimer. The active site has been analyzed by comparison to the structure of the aspartic protease, rhizopuspepsin, complexed with a peptide inhibitor. The HIV-1 protease is predicted to interact with seven residues ofthe protein substrate. This information can be used to design protease inhibitors and possible antivirual drugs.",

author = "Weber, {Irene T.} and Maria Miller and Mariusz Jask{\'o}lski and Jonathan Leis and Skalka, {Anna Marie} and Alexander Wlodawer",

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AU - Weber, Irene T.

AU - Miller, Maria

AU - Jaskólski, Mariusz

AU - Leis, Jonathan

AU - Skalka, Anna Marie

AU - Wlodawer, Alexander

PY - 1989

Y1 - 1989

N2 - The human immunodeficiency virus (HIV-1) encodes a protease that is essential for viral replication and is a member of the aspartic protease family. The recently determined three-dimensional structure of the related protease from Rous sarcoma virus has been used to model the smaller HIV-1 dimer. The active site has been analyzed by comparison to the structure of the aspartic protease, rhizopuspepsin, complexed with a peptide inhibitor. The HIV-1 protease is predicted to interact with seven residues ofthe protein substrate. This information can be used to design protease inhibitors and possible antivirual drugs.

AB - The human immunodeficiency virus (HIV-1) encodes a protease that is essential for viral replication and is a member of the aspartic protease family. The recently determined three-dimensional structure of the related protease from Rous sarcoma virus has been used to model the smaller HIV-1 dimer. The active site has been analyzed by comparison to the structure of the aspartic protease, rhizopuspepsin, complexed with a peptide inhibitor. The HIV-1 protease is predicted to interact with seven residues ofthe protein substrate. This information can be used to design protease inhibitors and possible antivirual drugs.

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ER -

Molecular modeling of the HIV-1 protease and its substrate binding site

Abstract

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