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PDBsum entry 1ddb
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Solution structure of the proapoptotic molecule bid: a structural basis for apoptotic agonists and antagonists.
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Authors
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J.M.Mcdonnell,
D.Fushman,
C.L.Milliman,
S.J.Korsmeyer,
D.Cowburn.
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Ref.
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Cell, 1999,
96,
625-634.
[DOI no: ]
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PubMed id
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Abstract
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Members of the BCL2 family of proteins are key regulators of programmed cell
death, acting either as apoptotic agonists or antagonists. Here we describe the
solution structure of BID, presenting the structure of a proapoptotic BCL2
family member. An analysis of sequence/structure of BCL2 family members allows
us to define a structural superfamily, which has implications for general
mechanisms for regulating proapoptotic activity. It appears two criteria must be
met for proapoptotic function within the BCL2 family: targeting of molecules to
intracellular membranes, and exposure of the BH3 death domain. BID's activity is
regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and
significantly changing the surface charge and hydrophobicity, resulting in a
change of cellular localization.
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Figure 4.
Figure 4. Comparison of BID and BCL-X[L] BH123 Acceptor
Region(a) The BID and (b) BCL-X[L]–BAK complex (PDB code 1lxl
[[49]) structures were colored according to surface
hydrophobicity (red for hydrophobic, white for hydrophilic)
using GRASP ( [44]). The backbone worms for both BID and the
BCL-X[L]–BAK BH3 peptide complex are colored yellow.
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Figure 5.
Figure 5. Predicted Structural Effects of the Caspase 8
Cleavage of BIDA ribbon diagram of (a) the full-length p22 BID
versus (b) the p15 tBID model (flexible loop BC and amino
terminus not shown). An analysis of the exposed hydrophobic
surface for (c) BID and (d) the tBID model presented in the same
orientation as in (a) and (b). Hydrophobic surfaces were
generated using GRASP ([44]); here the gray and yellow indicate
hydrophobic and hydrophilic surfaces, respectively.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1999,
96,
625-634)
copyright 1999.
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