4wmt | pdb_00004wmt
STRUCTURE OF MBP-MCL1 BOUND TO ligand 1 AT 2.35A
Structural highlights
FunctionMALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.MCL1_HUMAN Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis.[1] Publication Abstract from PubMedCrystallization 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. A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1.,Clifton MC, Dranow DM, Leed A, Fulroth B, Fairman JW, Abendroth J, Atkins KA, Wallace E, Fan D, Xu G, Ni ZJ, Daniels D, Van Drie J, Wei G, Burgin AB, Golub TR, Hubbard BK, Serrano-Wu MH PLoS One. 2015 Apr 24;10(4):e0125010. doi: 10.1371/journal.pone.0125010., eCollection 2015. PMID:25909780[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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