Solution structure of BID, an intracellular amplifier of apoptotic signaling

James J. Chou; Honglin Li; Guy S. Salvesen; Junying Yuan; Gerhard Wagner

doi:10.1016/S0092-8674(00)80572-3

Solution structure of BID, an intracellular amplifier of apoptotic signaling

James J. Chou, Honglin Li, Guy S. Salvesen, Junying Yuan, Gerhard Wagner

Research output: Contribution to journal › Article › peer-review

423 Scopus citations

Abstract

We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight α helices where two central hydrophobic helices a re surrounded by six amphipathic ones. The fold resembles pore-forming bacterial toxins and shows similarity to BCLX(L) although sequence homology to BCL-X(L) is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-X, and BID by aligning the BID and BAK BH3 motifs in the known BCL-X(L)-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage.

Original language	English (US)
Pages (from-to)	615-624
Number of pages	10
Journal	Cell
Volume	96
Issue number	5
DOIs	https://doi.org/10.1016/S0092-8674(00)80572-3
State	Published - Mar 5 1999
Externally published	Yes

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1016/S0092-8674(00)80572-3

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@article{13f25c08aaec4af594040c890053a000,

title = "Solution structure of BID, an intracellular amplifier of apoptotic signaling",

abstract = "We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight α helices where two central hydrophobic helices a re surrounded by six amphipathic ones. The fold resembles pore-forming bacterial toxins and shows similarity to BCLX(L) although sequence homology to BCL-X(L) is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-X, and BID by aligning the BID and BAK BH3 motifs in the known BCL-X(L)-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage.",

author = "Chou, {James J.} and Honglin Li and Salvesen, {Guy S.} and Junying Yuan and Gerhard Wagner",

note = "Funding Information: We thank Greg Heffron for help with the use of spectrometers and Alexey Lugovskoy for kind assistance in making the figures. This research was supported in part by a grant from the NIH (GM 38608 and GM 47467) to G. W., a grant from the Breast Cancer Program of the US Army to J. Y., and a postdoctoral fellowship to H. L. Acquisition and maintenance of spectrometers and computers used for this work were supported by NSF (MCB 9527181) and the Harvard Center for Structural Biology and the Giovanni Armenise-Harvard Foundation for Advanced Scientific Research. ",

year = "1999",

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doi = "10.1016/S0092-8674(00)80572-3",

language = "English (US)",

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T1 - Solution structure of BID, an intracellular amplifier of apoptotic signaling

AU - Chou, James J.

AU - Li, Honglin

AU - Salvesen, Guy S.

AU - Yuan, Junying

AU - Wagner, Gerhard

N1 - Funding Information: We thank Greg Heffron for help with the use of spectrometers and Alexey Lugovskoy for kind assistance in making the figures. This research was supported in part by a grant from the NIH (GM 38608 and GM 47467) to G. W., a grant from the Breast Cancer Program of the US Army to J. Y., and a postdoctoral fellowship to H. L. Acquisition and maintenance of spectrometers and computers used for this work were supported by NSF (MCB 9527181) and the Harvard Center for Structural Biology and the Giovanni Armenise-Harvard Foundation for Advanced Scientific Research.

PY - 1999/3/5

Y1 - 1999/3/5

N2 - We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight α helices where two central hydrophobic helices a re surrounded by six amphipathic ones. The fold resembles pore-forming bacterial toxins and shows similarity to BCLX(L) although sequence homology to BCL-X(L) is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-X, and BID by aligning the BID and BAK BH3 motifs in the known BCL-X(L)-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage.

AB - We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight α helices where two central hydrophobic helices a re surrounded by six amphipathic ones. The fold resembles pore-forming bacterial toxins and shows similarity to BCLX(L) although sequence homology to BCL-X(L) is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-X, and BID by aligning the BID and BAK BH3 motifs in the known BCL-X(L)-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage.

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JO - Cell

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Solution structure of BID, an intracellular amplifier of apoptotic signaling

Abstract

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