5ZZ4
Crystal structure of bruton's tyrosine kinase in complex with inhibitor 2e
Summary for 5ZZ4
| Entry DOI | 10.2210/pdb5zz4/pdb |
| Descriptor | Tyrosine-protein kinase BTK, N-[3-(4-amino-6-{[4-(morpholine-4-carbonyl)phenyl]amino}-1,3,5-triazin-2-yl)-2-methylphenyl]-4-tert-butylbenzamide (2 entities in total) |
| Functional Keywords | protein kinase, inhibitor complex, non-covalent, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 6 |
| Total formula weight | 190467.55 |
| Authors | Kawahata, W.,Asami, T.,Irie, T.,Kiyoi, T.,Taniguchi, H.,Asamitsu, Y.,Inoue, T.,Miyake, T.,Sawa, M. (deposition date: 2018-05-30, release date: 2018-09-26, Last modification date: 2023-11-22) |
| Primary citation | Kawahata, W.,Asami, T.,Kiyoi, T.,Irie, T.,Taniguchi, H.,Asamitsu, Y.,Inoue, T.,Miyake, T.,Sawa, M. Design and Synthesis of Novel Amino-triazine Analogues as Selective Bruton's Tyrosine Kinase Inhibitors for Treatment of Rheumatoid Arthritis. J. Med. Chem., 61:8917-8933, 2018 Cited by PubMed Abstract: Bruton's tyrosine kinase (BTK) is a promising drug target for the treatment of multiple diseases, such as B-cell malignances, asthma, and rheumatoid arthritis. A series of novel aminotriazines were identified as highly selective inhibitors of BTK by a scaffold-hopping approach. Subsequent SAR studies of this series using two conformationally different BTK proteins, an activated form of BTK and an unactivated form of BTK, led to the discovery of a highly selective BTK inhibitor, 4b. With significant efficacy in models in vivo and good ADME and safety profiles, 4b was advanced into preclinical studies. PubMed: 30216722DOI: 10.1021/acs.jmedchem.8b01147 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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