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PDBsum entry 2g5b
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* Residue conservation analysis
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PDB id:
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Apoptosis
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Title:
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Crystal structure of the anti-bax monoclonal antibody 6a7 and a bax peptide.
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Structure:
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6a7 fab light chain. Chain: a, c, e, g. Engineered: yes. 6a7 fab heavy chain. Chain: b, d, f, h. Engineered: yes. Bax peptide. Chain: i, j, k, l. Fragment: bax peptide fragment.
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: mus musculus. Expression_system_taxid: 10090. Synthetic: yes. Other_details: this sequence occurs naturally in mice and humans
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Biol. unit:
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Trimer (from
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Resolution:
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2.30Å
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R-factor:
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0.234
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R-free:
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0.275
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Authors:
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F.W.Peyerl,S.Dai,G.A.Murphy,P.Marrack,J.W.Kappler
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Key ref:
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F.W.Peyerl
et al.
(2007).
Elucidation of some Bax conformational changes through crystallization of an antibody-peptide complex.
Cell Death Differ,
14,
447-452.
PubMed id:
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Date:
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22-Feb-06
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Release date:
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25-Jul-06
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PROCHECK
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Headers
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References
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Cell Death Differ
14:447-452
(2007)
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PubMed id:
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Elucidation of some Bax conformational changes through crystallization of an antibody-peptide complex.
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F.W.Peyerl,
S.Dai,
G.A.Murphy,
F.Crawford,
J.White,
P.Marrack,
J.W.Kappler.
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ABSTRACT
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The Bcl-2 family member Bax plays a critical role in apoptosis. In healthy
resting cells, Bax resides in the cytoplasm and loosely attached to the
mitochondrial membrane. Apoptotic stimuli induce Bax activation, which is
characterized by translocation and multimerization on the mitochondrial membrane
surface resulting in exposure of an amino terminal epitope recognized by the
monoclonal antibody 6A7. To understand the structural changes that occur during
Bax activation, we determined the crystal structure of a Bax peptide bound to
the 6A7 Fab fragment to a resolution of 2.3 A. The structure reveals the
conformation of the 6A7 peptide epitope on Bax in the activated form and
elucidates the extensive structural changes that Bax must undergo during the
conversion from its native to its activated conformation.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.Westphal,
G.Dewson,
P.E.Czabotar,
and
R.M.Kluck
(2011).
Molecular biology of Bax and Bak activation and action.
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Biochim Biophys Acta,
1813,
521-531.
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Z.Zhang,
T.Song,
T.Zhang,
J.Gao,
G.Wu,
L.An,
and
G.Du
(2011).
A novel BH3 mimetic S1 potently induces Bax/Bak-dependent apoptosis by targeting both Bcl-2 and Mcl-1.
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Int J Cancer,
128,
1724-1735.
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H.Düssmann,
M.Rehm,
C.G.Concannon,
S.Anguissola,
M.Würstle,
S.Kacmar,
P.Völler,
H.J.Huber,
and
J.H.Prehn
(2010).
Single-cell quantification of Bax activation and mathematical modelling suggest pore formation on minimal mitochondrial Bax accumulation.
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Cell Death Differ,
17,
278-290.
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F.Radogna,
S.Cristofanon,
L.Paternoster,
M.D'Alessio,
M.De Nicola,
C.Cerella,
M.Dicato,
M.Diederich,
and
L.Ghibelli
(2008).
Melatonin antagonizes the intrinsic pathway of apoptosis via mitochondrial targeting of Bcl-2.
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J Pineal Res,
44,
316-325.
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J.L.Alabran,
A.Cheuk,
K.Liby,
M.Sporn,
J.Khan,
J.Letterio,
and
K.S.Leskov
(2008).
Human neuroblastoma cells rapidly enter cell cycle arrest and apoptosis following exposure to C-28 derivatives of the synthetic triterpenoid CDDO.
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Cancer Biol Ther,
7,
709-717.
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L.P.Billen,
A.Shamas-Din,
and
D.W.Andrews
(2008).
Bid: a Bax-like BH3 protein.
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Oncogene,
27,
S93-104.
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R.J.Youle,
and
A.Strasser
(2008).
The BCL-2 protein family: opposing activities that mediate cell death.
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Nat Rev Mol Cell Biol,
9,
47-59.
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H.Arokium,
H.Ouerfelli,
G.Velours,
N.Camougrand,
F.M.Vallette,
and
S.Manon
(2007).
Substitutions of potentially phosphorylatable serine residues of Bax reveal how they may regulate its interaction with mitochondria.
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J Biol Chem,
282,
35104-35112.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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