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Bcl-xL is a major inhibitor of apoptosis, a fundamental homeostatic process of programmed cell death that is highly conserved across evolution. Because it plays prominent roles in cancer, Bcl-xL is a major target for anticancer therapy and for studies aimed at understanding its structure and activity. Although Bcl-xL is active primarily at intracellular membranes, most studies have focused on soluble forms of the protein lacking both the membrane-anchoring C-terminal tail and the intrinsically disordered loop, and this has resulted in a fragmented view of the protein's biological activity. Here, we describe the conformation of full-length Bcl-xL. Using NMR spectroscopy, molecular dynamics simulations, and isothermal titration calorimetry, we show how the three structural elements affect the protein's structure, dynamics, and ligand-binding activity in both its soluble and membrane-anchored states. The combined data provide information about the molecular basis for the protein's functionality and a view of its complex molecular mechanisms. Copyright © 2020 Biophysical Society. Published by Elsevier Inc. All rights reserved.


Pavel Ryzhov, Ye Tian, Yong Yao, Andrey A Bobkov, Wonpil Im, Francesca M Marassi. Conformational States of the Cytoprotective Protein Bcl-xL. Biophysical journal. 2020 Oct 06;119(7):1324-1334

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PMID: 32888404

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