3LIX
crystal structure of htlv protease complexed with the inhibitor KNI-10729
Summary for 3LIX
| Entry DOI | 10.2210/pdb3lix/pdb |
| Related | 2B7F 3LIN 3LIQ 3LIT 3LIV 3LIY |
| Related PRD ID | PRD_000581 |
| Descriptor | Protease, ZINC ION, N-{(1S,2S)-1-benzyl-3-[(4R)-5,5-dimethyl-4-{[(1R)-1,2,2-trimethylpropyl]carbamoyl}-1,3-thiazolidin-3-yl]-2-hydroxy-3-oxopropyl}-3-methyl-N~2~-{(2S)-2-[(morpholin-4-ylacetyl)amino]-2-phenylacetyl}-L-valinamide, ... (4 entities in total) |
| Functional Keywords | hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Human T-lymphotropic virus 1 |
| Total number of polymer chains | 2 |
| Total formula weight | 25993.61 |
| Authors | Satoh, T.,Li, M.,Nguyen, J.,Kiso, Y.,Wlodawer, A.,Gustchina, A. (deposition date: 2010-01-25, release date: 2010-07-14, Last modification date: 2023-09-06) |
| Primary citation | Satoh, T.,Li, M.,Nguyen, J.T.,Kiso, Y.,Gustchina, A.,Wlodawer, A. Crystal structures of inhibitor complexes of human T-cell leukemia virus (HTLV-1) protease. J.Mol.Biol., 401:626-641, 2010 Cited by PubMed Abstract: Human 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. PubMed: 20600105DOI: 10.1016/j.jmb.2010.06.052 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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