MOLECULAR MODELING OF THE HIV-1 PROTEASE AND ITS SUBSTRATE BINDING-SITE
MOLECULAR MODELING OF THE HIV-1 PROTEASE AND ITS SUBSTRATE BINDING-SITE
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DOI：
10.1126/science.2537531
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发表时间：
1989-02-17
期刊：
影响因子：
56.9
通讯作者：
WLODAWER, A
中科院分区：
文献类型：
--
作者：
WEBER, IT;MILLER, M;WLODAWER, A
人类免疫缺陷病毒（HIV - 1）编码一种对病毒复制至关重要的蛋白酶，它是天冬氨酸蛋白酶家族的成员。最近确定的劳斯肉瘤病毒相关蛋白酶的三维结构已被用于构建较小的HIV - 1二聚体模型。通过与天冬氨酸蛋白酶（根霉胃蛋白酶）与一种肽抑制剂形成的复合物结构进行比较，对活性位点进行了分析。预计HIV - 1蛋白酶会与蛋白质底物的7个残基相互作用。这些信息可用于设计蛋白酶抑制剂以及可能的抗病毒药物。
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 of the protein substrate. This information can be used to design protease inhibitors and possible antivirual drugs.