Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/95496
Title: X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
Authors: Yoon, Ho Sup
Sattler, Michael
Muchmore, Steven W.
Liang, Heng
Meadows, Robert P.
Harlan, John E.
Nettesheim, David G.
Chang, Brian S.
Thompson, Craig B.
Wong, Sui-Lam
Ng, Shi-Chung
Fesik, Stephen W.
Keywords: DRNTU::Science::Biological sciences
Issue Date: 1996
Source: Muchmore, S. W., Sattler, M., Liang, H., Meadows, R. P., Harlan, J. E., Yoon, H. S., et al. (1996). X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature, 381, 335-341.
Series/Report no.: Nature
Abstract: THE Bcl-2 family of proteins regulate programmed cell death by an unknown mechanism1. Here we describe the crystal and solution structures of a Bcl-2 family member, Bcl-xL (ref. 2). The structures consist of two central, primarily hydrophobic α-helices, which are surrounded by amphipathic helices. A 60-residue loop connecting helices αl and α2 was found to be flexible and non-essential for anti-apoptotic activity. The three functionally important Bcl-2 homology regions (BH1, BH2 and BH3)3–5 are in close spatial proximity and form an elongated hydrophobic cleft that may represent the binding site for other Bcl-2 family members. The arrangement of the α-helices in Bcl-xL is reminiscent of the membrane translocation domain of bacterial toxins, in particular diphtheria toxin and the colicins6. The structural similarity may provide a clue to the mechanism of action of the Bcl-2 family of proteins.
URI: https://hdl.handle.net/10356/95496
http://hdl.handle.net/10220/8302
DOI: 10.1038/381335a0
Rights: © 1996 Nature Publishing Group. This is the author created version of a work that has been peer reviewed and accepted for publication by Nature, Nature Publishing Group. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [DOI: http://dx.doi.org/10.1038/381335a0 ]
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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