6LMI
Crystal structure of HIV-1 integrase catalytic core domain in complex with 2-(tert-butoxy)-2-[3-(3,4-dihydro-2H-1-benzopyran-6-yl)-6-methanesulfonamido-2,3',4',5-tetramethyl-[1,1'-biphenyl]-4-yl]acetic acid
Summary for 6LMI
| Entry DOI | 10.2210/pdb6lmi/pdb |
| Descriptor | Integrase catalytic, SULFATE ION, TRIETHYLENE GLYCOL, ... (6 entities in total) |
| Functional Keywords | hydrolase transferase/inhibitor, transferase |
| Biological source | Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1) |
| Total number of polymer chains | 1 |
| Total formula weight | 19404.81 |
| Authors | Sugiyama, S.,Iwaki, T.,Tamura, Y.,Tomita, K.,Matsuoka, E.,Arita, S.,Seki, T.,Yoshinaga, T.,Kawasuji, T. (deposition date: 2019-12-25, release date: 2020-09-23, Last modification date: 2024-11-06) |
| Primary citation | Sugiyama, S.,Iwaki, T.,Tamura, Y.,Tomita, K.,Matsuoka, E.,Arita, S.,Seki, T.,Yoshinaga, T.,Kawasuji, T. Discovery of novel integrase-LEDGF/p75 allosteric inhibitors based on a benzene scaffold. Bioorg.Med.Chem., 28:115643-115643, 2020 Cited by PubMed Abstract: We report herein the discovery of novel integrase-LEDGF/p75 allosteric inhibitors (INLAIs) based on a benzene scaffold 3. This scaffold can extend substituents from the C1 position unlike the common pyridine scaffolds 2. Structure-activity relationship studies showed that the sulfonamide linker at the C1 position was important for the antiviral activity. Interaction between sulfonamide and Q95 was observed by X-ray crystallography. Compound 31h showed more potent antiviral activity (EC (NL432) = 3.9 nM) than BI-224436 (EC (NL432) = 56 nM), suggesting the potential of the newly designed scaffold 3. PubMed: 32773094DOI: 10.1016/j.bmc.2020.115643 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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