3lit
The crystal structure of htlv protease complexed with the inhibitor KNI-10681The crystal structure of htlv protease complexed with the inhibitor KNI-10681
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman T-cell leukemia virus type 1 (HTLV-1) is a retrovirus associated with several serious diseases, such as adult T-cell leukemia and tropical spastic paraparesis/myelopathy. For a number of years, the protease (PR) encoded by HTLV-1 has been a target for designing antiviral drugs, but that effort was hampered by limited available structural information. We report a high-resolution crystal structure of HTLV-1 PR complexed with a statine-containing inhibitor, a significant improvement over the previously available moderate-resolution structure. We also report crystal structures of the complexes of HTLV-1 PR with five different inhibitors that are more compact and more potent. A detailed study of structure-activity relationships was performed to interpret in detail the influence of the polar and hydrophobic interactions between the inhibitors and the protease. Crystal structures of inhibitor complexes of human T-cell leukemia virus (HTLV-1) protease.,Satoh T, Li M, Nguyen JT, Kiso Y, Gustchina A, Wlodawer A J Mol Biol. 2010 Aug 27;401(4):626-41. Epub 2010 Jun 30. PMID:20600105[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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