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PDBsum entry 1cdf

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Receptor PDB id
1cdf

 

 

 

 

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Contents
Protein chain
121 a.a.
Theoretical model
PDB id:
1cdf
Name: Receptor
Title: Three-dimensional theoretical model of the ligand binding domain of the human b cell recptor cd40
Structure: B-cell surface antigen cd40. Chain: null. Fragment: extracellular region, residues 24 - 144
Source: Homo sapiens. Human
Authors: J.Bajorath
Key ref: J.Bajorath and A.Aruffo (1997). Construction and analysis of a detailed three-dimensional model of the ligand binding domain of the human B cell receptor CD40. Proteins, 27, 59-70. PubMed id: 9037712
Date:
26-Mar-96     Release date:   01-Apr-97    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 121 a.a.
Key:    Secondary structure

 

 
Proteins 27:59-70 (1997)
PubMed id: 9037712  
 
 
Construction and analysis of a detailed three-dimensional model of the ligand binding domain of the human B cell receptor CD40.
J.Bajorath, A.Aruffo.
 
  ABSTRACT  
 
The interaction between the human B cell receptor CD40 and its ligand on T cells is critical for B cell proliferation and the regulation of humoral immune responses. CD40 is a member of the tumor necrosis factor receptor (TNFR) family. We report here the construction and analysis of a detailed three-dimensional model of the TNFR-homologous extracellular region of CD40. This study provides an example for structure-based model building in the presence of low sequence similarity. The assessment of model quality and sequence-structure compatibility is emphasized, and limitations of the model are discussed. The current CD40 model predicts structural details beyond the backbone level. Features of the CD40 ligand binding site are discussed in conjunction with the results of a previous mutagenesis study.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17504764 C.Reyes-Moreno, E.Sharif-Askari, J.Girouard, C.Léveillé, M.Jundi, A.Akoum, R.Lapointe, A.Darveau, and W.Mourad (2007).
Requirement of oxidation-dependent CD40 homodimers for CD154/CD40 bidirectional signaling.
  J Biol Chem, 282, 19473-19480.  
14681401 J.Kopp, and T.Schwede (2004).
The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models.
  Nucleic Acids Res, 32, D230-D234.  
11232332 S.M.McWhirter, S.S.Pullen, B.G.Werneburg, M.E.Labadia, R.H.Ingraham, J.J.Crute, M.R.Kehry, and T.Alber (1999).
Structural and biochemical analysis of signal transduction by the TRAF family of adapter proteins.
  Cold Spring Harb Symp Quant Biol, 64, 551-562.  
10411888 S.M.McWhirter, S.S.Pullen, J.M.Holton, J.J.Crute, M.R.Kehry, and T.Alber (1999).
Crystallographic analysis of CD40 recognition and signaling by human TRAF2.
  Proc Natl Acad Sci U S A, 96, 8408-8413.
PDB code: 1qsc
9733755 J.Bajorath (1998).
Detailed comparison of two molecular models of the human CD40 ligand with an x-ray structure and critical assessment of model-based mutagenesis and residue mapping studies.
  J Biol Chem, 273, 24603-24609.  
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. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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