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Immune system PDB-id
2q86
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Contents
Description
Header details
Header records
References
PROCHECK
Protein chains
189 a.a. *
233 a.a. *
Ligands
NAG-NAG-BMA-MAN-
FUC

NAG
NAG-NAG-BMA-FUC
Waters ×546

* Residue conservation analysis
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PDB id: 2q86
Name: Immune system
Title: Structure of the mouse invariant nkt cell receptor valpha14

Structure:
Valpha14 tcr. Chain: a, c. Fragment: extracellular domain. Engineered: yes. Mutation: yes. Vbeta8.2. Chain: b, d. Fragment: extracellular domain. Engineered: yes.

Source:
Mus musculus. House mouse. Organism_taxid: 10090. Gene: valpha14. Expressed in: drosophila melanogaster. Expression_system_taxid: 7227. Gene: vbeta8.2.

UniProt:
Chains A, C: P01849 (TCA_MOUSE)
Pfam  
Seq: 138 a.a.
Struc: 189 a.a.*

Chains B, D: P01852 (TCB1_MOUSE)
Pfam  
Seq:
Struc:
Seq: 173 a.a.
Struc: 233 a.a.*
Key:    PfamA domain
 Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Resolution:
1.85Å

R-factor:
0.180

R-free:
0.223

Authors:
D.M.Zajonc

Key ref:
D.M.Zajonc et al. (2008). Crystal structures of mouse CD1d-iGb3 complex and its cognate Valpha14 T cell receptor suggest a model for dual recognition of foreign and self glycolipids.. J Mol Biol, 377, 1104-1116. [PubMed id: 18295796] [DOI: 10.1016/j.jmb.2008.01.061]

Date:
08-Jun-07

Release date:
01-Apr-08

Related entries:
2eyr
structure of the human homolog va24
2cde
structure of the human homolog va24
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    Key reference    
 
 
DOI no: 10.1016/j.jmb.2008.01.061 J Mol Biol 377:1104-1116 (2008)
PubMed id: 18295796  
 
 
Crystal structures of mouse CD1d-iGb3 complex and its cognate Valpha14 T cell receptor suggest a model for dual recognition of foreign and self glycolipids.
D.M.Zajonc, P.B.Savage, A.Bendelac, I.A.Wilson, L.Teyton.
 
  ABSTRACT  
 
The semi-invariant Valpha14Jalpha18 T cell receptor (TCR) is expressed by regulatory NKT cells and has the unique ability to recognize chemically diverse ligands presented by CD1d. The crystal structure of CD1d complexed to a natural, endogenous ligand, isoglobotrihexosylceramide (iGb3), illustrates the extent of this diversity when compared to the binding of potent, exogenous ligands, such as alpha-galactosylceramide (alpha-GalCer). A single mode of recognition for these two classes of ligands would then appear problematic for a single T cell receptor. However, the Valpha14 TCR adopts two different conformations in the crystal where, in one configuration, the presence of a larger cavity between the two CDR3 regions could accommodate iGb3 and, in the other, a smaller cavity fits alpha-GalCer more snugly. Alternatively, the extended iGb3 headgroup could be "squashed" upon docking of the TCR and accommodated between the CD1 and TCR surfaces. Thus, the same TCR may adopt alternative modes of recognition for these foreign and self-ligands for NKT cell activation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19415116 D.Cox, L.Fox, R.Tian, W.Bardet, M.Skaley, D.Mojsilovic, J.Gumperz, and W.Hildebrand (2009).
Determination of cellular lipids bound to human CD1d molecules.
  PLoS ONE, 4, e5325.  
19594637 D.M.Zajonc, and M.Kronenberg (2009).
Carbohydrate specificity of the recognition of diverse glycolipids by natural killer T cells.
  Immunol Rev, 230, 188-200.  
19476512 M.Boes, A.J.Stoppelenburg, and F.C.Sillé (2009).
Endosomal processing for antigen presentation mediated by CD1 and Class I major histocompatibility complex: roads to display or destruction.
  Immunology, 127, 163-170.  
19079136 V.Cerundolo, J.D.Silk, S.H.Masri, and M.Salio (2009).
Harnessing invariant NKT cells in vaccination strategies.
  Nat Rev Immunol, 9, 28-38.  
19004781 D.M.Zajonc, H.Striegl, C.C.Dascher, and I.A.Wilson (2008).
The crystal structure of avian CD1 reveals a smaller, more primordial antigen-binding pocket compared to mammalian CD1.
  Proc Natl Acad Sci U S A, 105, 17925-17930.
PDB code: 3dbx
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.