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PDBsum entry 2g5b

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Apoptosis PDB id
2g5b

 

 

 

 

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Contents
Protein chains
217 a.a. *
216 a.a. *
Ligands
PRO-THR-SER-SER-
GLU-GLN-ILE
×4
NAG-NAG-BMA ×2
NAG-NDG
NAG-NAG-MAN
SO4 ×7
Waters ×422
* Residue conservation analysis
PDB id:
2g5b
Name: Apoptosis
Title: Crystal structure of the anti-bax monoclonal antibody 6a7 and a bax peptide.
Structure: 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.
Source: 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
Biol. unit: Trimer (from PQS)
Resolution:
2.30Å     R-factor:   0.234     R-free:   0.275
Authors: F.W.Peyerl,S.Dai,G.A.Murphy,P.Marrack,J.W.Kappler
Key ref: 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: 16946732
Date:
22-Feb-06     Release date:   25-Jul-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
No UniProt id for this chain
Struc: 217 a.a.
Protein chains
Pfam   ArchSchema ?
P84751  (HVM63_MOUSE) -  Ig heavy chain Mem5 (Fragment) from Mus musculus
Seq:
Struc:
237 a.a.
216 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 35 residue positions (black crosses)

 

 
Cell Death Differ 14:447-452 (2007)
PubMed id: 16946732  
 
 
Elucidation of some Bax conformational changes through crystallization of an antibody-peptide complex.
F.W.Peyerl, S.Dai, G.A.Murphy, F.Crawford, J.White, P.Marrack, J.W.Kappler.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21195116 D.Westphal, G.Dewson, P.E.Czabotar, and R.M.Kluck (2011).
Molecular biology of Bax and Bak activation and action.
  Biochim Biophys Acta, 1813, 521-531.  
20503275 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.
  Int J Cancer, 128, 1724-1735.  
19745831 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.
  Cell Death Differ, 17, 278-290.  
18339127 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.
  J Pineal Res, 44, 316-325.  
  18277094 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.
  Cancer Biol Ther, 7, 709-717.  
19641510 L.P.Billen, A.Shamas-Din, and D.W.Andrews (2008).
Bid: a Bax-like BH3 protein.
  Oncogene, 27, S93-104.  
18097445 R.J.Youle, and A.Strasser (2008).
The BCL-2 protein family: opposing activities that mediate cell death.
  Nat Rev Mol Cell Biol, 9, 47-59.  
17911107 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.
  J Biol Chem, 282, 35104-35112.  
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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