4WMX

The structure of MBP-MCL1 bound to ligand 6 at 2.0A

Summary for 4WMX

• Entry DOI: 10.2210/pdb4wmx/pdb
• Related: 4WMR 4WMS 4WMT 4WMU 4WMV 4WMW
• Related PRD ID: PRD_900001
• Descriptor: MBP-MCL1 chimera protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, 4-ethenyl-2-[(phenylsulfonyl)amino]benzoic acid, ... (6 entities in total)
• Functional Keywords: apoptosis, protein-protein interaction
• Biological source: Escherichia coli; More
• Total number of polymer chains: 1
• Total formula weight: 58441.07

Authors

Clifton, M.C.,Dranow, D.M. (deposition date: 2014-10-09, release date: 2015-05-06, Last modification date: 2023-09-27)

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

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: 25909780
DOI: 10.1371/journal.pone.0125010

Experimental method

X-RAY DIFFRACTION (2 Å)