8EL1
Structure of MBP-Mcl-1 in complex with ABBV-467
Summary for 8EL1
| Entry DOI | 10.2210/pdb8el1/pdb |
| Related | 8EKX 8EL0 |
| Descriptor | Maltose/maltodextrin-binding periplasmic protein,Induced myeloid leukemia cell differentiation protein Mcl-1, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, (7R,16R)-19,23-dichloro-10-{[2-(4-{[(2R)-1,4-dioxan-2-yl]methoxy}phenyl)pyrimidin-4-yl]methoxy}-1-(4-fluorophenyl)-20,22-dimethyl-16-[(4-methylpiperazin-1-yl)methyl]-7,8,15,16-tetrahydro-18,21-etheno-13,9-(metheno)-6,14,17-trioxa-2-thia-3,5-diazacyclononadeca[1,2,3-cd]indene-7-carboxylic acid, ... (4 entities in total) |
| Functional Keywords | mbp-mcl-1 fusion protein, apoptosis, inhibitor complex, abbv-467 |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 242068.62 |
| Authors | Judge, R.A.,Judd, A.S.,Souers, A.J. (deposition date: 2022-09-22, release date: 2023-10-25, Last modification date: 2023-11-08) |
| Primary citation | Yuda, J.,Will, C.,Phillips, D.C.,Abraham, L.,Alvey, C.,Avigdor, A.,Buck, W.,Besenhofer, L.,Boghaert, E.,Cheng, D.,Cojocari, D.,Doyle, K.,Hansen, T.M.,Huang, K.,Johnson, E.F.,Judd, A.S.,Judge, R.A.,Kalvass, J.C.,Kunzer, A.,Lam, L.T.,Li, R.,Martin, R.L.,Mastracchio, A.,Mitten, M.,Petrich, A.,Wang, J.,Ward, J.E.,Zhang, H.,Wang, X.,Wolff, J.E.,Bell-McGuinn, K.M.,Souers, A.J. Selective MCL-1 inhibitor ABBV-467 is efficacious in tumor models but is associated with cardiac troponin increases in patients. Commun Med (Lond), 3:154-154, 2023 Cited by PubMed Abstract: MCL-1 is a prosurvival B-cell lymphoma 2 family protein that plays a critical role in tumor maintenance and survival and can act as a resistance factor to multiple anticancer therapies. Herein, we describe the generation and characterization of the highly potent and selective MCL-1 inhibitor ABBV-467 and present findings from a first-in-human trial that included patients with relapsed/refractory multiple myeloma (NCT04178902). PubMed: 37880389DOI: 10.1038/s43856-023-00380-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.406 Å) |
Structure validation
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