2bid: Difference between revisions

Revision as of 17:38, 21 February 2008

HUMAN PRO-APOPTOTIC PROTEIN BID

OverviewOverview

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 alpha helices where two central hydrophobic helices are surrounded by six amphipathic ones. The fold resembles poreforming bacterial toxins and shows similarity to BCL-XL although sequence homology to BCL-XL is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-XL and BID by aligning the BID and BAK BH3 motifs in the known BCL-XL-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.

About this StructureAbout this Structure

2BID is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure of BID, an intracellular amplifier of apoptotic signaling., Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G, Cell. 1999 Mar 5;96(5):615-24. PMID:10089877

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OCA

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 ==Overview==
-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 alpha helices where, two central hydrophobic helices are surrounded by six amphipathic ones., The fold resembles poreforming bacterial toxins and shows similarity to, BCL-XL although sequence homology to BCL-XL is limited to the 16-residue, BH3 domain. Furthermore, we modeled a complex of BCL-XL and BID by, aligning the BID and BAK BH3 motifs in the known BCL-XL-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.
+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 alpha helices where two central hydrophobic helices are surrounded by six amphipathic ones. The fold resembles poreforming bacterial toxins and shows similarity to BCL-XL although sequence homology to BCL-XL is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-XL and BID by aligning the BID and BAK BH3 motifs in the known BCL-XL-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.
 ==About this Structure==
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 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Chou, J.J.]]
+[[Category: Chou, J J.]]
 [[Category: Li, H.]]
-[[Category: Salvesen, G.S.]]
+[[Category: Salvesen, G S.]]
 [[Category: Wagner, G.]]
 [[Category: Yuan, J.]]
@@ Line 21: / Line 21: @@
 [[Category: programmed cell death]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:16:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:10 2008''