4YDG
Crystal structure of compound 10 in complex with HTLV-1 Protease
Summary for 4YDG
| Entry DOI | 10.2210/pdb4ydg/pdb |
| Related | 3LIX 3WSJ |
| Descriptor | HTLV-1 protease, SULFATE ION, N,N'-(3S,4S)-PYRROLIDINE-3,4-DIYLBIS(4-AMINO-N-BENZYLBENZENESULFONAMIDE) (3 entities in total) |
| Functional Keywords | htlv-1 protease, hydrolase |
| Biological source | Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1) |
| Cellular location | Matrix protein p19: Virion . Capsid protein p24: Virion . Nucleocapsid protein p15-pro: Virion : P03362 |
| Total number of polymer chains | 2 |
| Total formula weight | 25917.03 |
| Authors | Kuhnert, M.,Blum, A.,Steuber, H.,Diederich, W.E. (deposition date: 2015-02-22, release date: 2016-02-03, Last modification date: 2024-01-10) |
| Primary citation | Kuhnert, M.,Blum, A.,Steuber, H.,Diederich, W.E. Privileged Structures Meet Human T-Cell Leukemia Virus-1 (HTLV-1): C2-Symmetric 3,4-Disubstituted Pyrrolidines as Nonpeptidic HTLV-1 Protease Inhibitors. J.Med.Chem., 58:4845-4850, 2015 Cited by PubMed Abstract: 3,4-disubstituted pyrrolidines originally designed to inhibit the closely related HIV-1 protease were evaluated as privileged structures against HTLV-1 protease (HTLV-1 PR). The most potent inhibitor of this series exhibits two-digit nanomolar affinity and represents, to the best of our knowledge, the most potent nonpeptidic inhibitor of HTLV-1 PR described so far. The X-ray structures of two representatives bound to HTLV-1 PR were determined, and the structural basis of their affinity is discussed. PubMed: 26000468DOI: 10.1021/acs.jmedchem.5b00346 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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