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Public Library of Science, PLoS ONE, 4(10), p. e0125010, 2015

DOI: 10.1371/journal.pone.0125010

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A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1

Journal article published in 2015 by Matthew C. Clifton, David M. Dranow, Alison Leed, Ben Fulroth, James W. Fairman, Jan Abendroth, Kateri A. Atkins, Ellen Wallace, Dazhong Fan, Guoping Xu, Z. J. Ni, Doug Daniels ORCID, John Van Drie, Guo Wei, Alex B. Burgin and other authors.
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.