4WMR
STRUCTURE OF MCL1 BOUND TO BRD inhibitor ligand 1 AT 1.7A
Summary for 4WMR
Entry DOI | 10.2210/pdb4wmr/pdb |
Related | 4WMS 4WMT 4WMU 4WMV 4WMW 4WMX |
Descriptor | Induced myeloid leukemia cell differentiation protein Mcl-1, ZINC ION, 7-[2-(1H-imidazol-1-yl)-4-methylpyridin-3-yl]-3-[3-(naphthalen-1-yloxy)propyl]-1-[2-oxo-2-(piperazin-1-yl)ethyl]-1H-indole-2-carboxylic acid, ... (5 entities in total) |
Functional Keywords | apoptosis, protein-protein interaction, apoptosis-inhibitor complex, apoptosis/inhibitor |
Biological source | Homo sapiens (Human) |
Cellular location | Membrane ; Single-pass membrane protein : Q07820 |
Total number of polymer chains | 1 |
Total formula weight | 18341.51 |
Authors | CLIFTON, M.C.,EDWARDS, T.E. (deposition date: 2014-10-09, release date: 2015-05-06, Last modification date: 2023-12-27) |
Primary citation | Clifton, M.C.,Dranow, D.M.,Leed, A.,Fulroth, B.,Fairman, J.W.,Abendroth, J.,Atkins, K.A.,Wallace, E.,Fan, D.,Xu, G.,Ni, Z.J.,Daniels, D.,Van Drie, J.,Wei, G.,Burgin, A.B.,Golub, T.R.,Hubbard, B.K.,Serrano-Wu, M.H. A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1. Plos One, 10:e0125010-e0125010, 2015 Cited by PubMed Abstract: Crystallization of a maltose-binding protein MCL1 fusion has yielded a robust crystallography platform that generated the first apo MCL1 crystal structure, as well as five ligand-bound structures. The ability to obtain fragment-bound structures advances structure-based drug design efforts that, despite considerable effort, had previously been intractable by crystallography. In the ligand-independent crystal form we identify inhibitor binding modes not observed in earlier crystallographic systems. This MBP-MCL1 construct dramatically improves the structural understanding of well-validated MCL1 ligands, and will likely catalyze the structure-based optimization of high affinity MCL1 inhibitors. PubMed: 25909780DOI: 10.1371/journal.pone.0125010 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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