2bid
From Proteopedia
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| - | [[Image:2bid.jpg|left|200px]] | + | [[Image:2bid.jpg|left|200px]] |
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| - | '''HUMAN PRO-APOPTOTIC PROTEIN BID''' | + | {{Structure |
| + | |PDB= 2bid |SIZE=350|CAPTION= <scene name='initialview01'>2bid</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN PRO-APOPTOTIC PROTEIN BID''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BID is a [ | + | 2BID is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BID OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10089877 10089877] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: programmed cell death]] | [[Category: programmed cell death]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:02:22 2008'' |
Revision as of 14:02, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN PRO-APOPTOTIC PROTEIN BID
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.
About this Structure
2BID is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 16:02:22 2008
