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PDBsum entry 1bzi
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protein Protein-protein interface(s) links
Complex (fas/ligand) PDB id
1bzi

 

 

 

 

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Contents
Protein chains
81 a.a.
106 a.a.
Theoretical model
PDB id:
1bzi
Name: Complex (fas/ligand)
Title: Theoretical model of the cd95-ligand complex
Structure: Fas. Chain: a. Fragment: extracellular region. Fas antigen ligand. Chain: b, c. Fragment: extracellular region
Source: Homo sapiens. Human. Human
Authors: J.Bajorath
Key ref: J.Bajorath (1999). Analysis of Fas-ligand interactions using a molecular model of the receptor-ligand interface. J Comput Aided Mol Des, 13, 409-418. PubMed id: 10425605
Date:
29-Oct-98     Release date:   22-Jul-99    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 81 a.a.
Protein chains
No UniProt id for this chain
Struc: 106 a.a.
Key:    Secondary structure

 

 
J Comput Aided Mol Des 13:409-418 (1999)
PubMed id: 10425605  
 
 
Analysis of Fas-ligand interactions using a molecular model of the receptor-ligand interface.
J.Bajorath.
 
  ABSTRACT  
 
A molecular model of the complex between Fas and its ligand was generated to better understand the location and putative effects of site-specific mutations, analyze interactions at the Fas-FasL interface, and identify contact residues. The modeling study was conservative in the sense that regions in Fas and its ligand which could not be predicted with confidence were omitted from the model to ensure accuracy of the analysis. Using the model, it was possible to map four of five N-linked glycosylation sites in Fas and FasL and to study 10 of 11 residues previously identified by mutagenesis as important for binding. Interactions involving six of these residues could be analyzed in detail and their importance for binding was rationalized based on the model. The predicted structure of the Fas-FasL interface was consistent with the experimentally established importance of these residues for binding. In addition, five previously not targeted residues were identified and predicted to contribute to binding via electrostatic interactions. Despite its limitations, the study provided a much improved basis to understand the role of Fas and FasL residues for binding compared to previous residue mapping studies using only a molecular model of Fas.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19114018 M.Voss, M.Lettau, M.Paulsen, and O.Janssen (2008).
Posttranslational regulation of Fas ligand function.
  Cell Commun Signal, 6, 11.  
17544837 Y.Li, X.Yang, A.H.Nguyen, and I.Brockhausen (2007).
Requirement of N-glycosylation for the secretion of recombinant extracellular domain of human Fas in HeLa cells.
  Int J Biochem Cell Biol, 39, 1625-1636.  
15084739 A.Hasegawa, X.Cheng, K.Kajino, A.Berezov, K.Murata, T.Nakayama, H.Yagita, R.Murali, and M.I.Greene (2004).
Fas-disabling small exocyclic peptide mimetics limit apoptosis by an unexpected mechanism.
  Proc Natl Acad Sci U S A, 101, 6599-6604.  
12371937 S.Tsuyuki, M.Kono, and E.T.Bloom (2002).
Cloning and potential utility of porcine Fas ligand: overexpression in porcine endothelial cells protects them from attack by human cytolytic cells.
  Xenotransplantation, 9, 410-421.  
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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