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PDBsum entry 2qqq

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protein Protein-protein interface(s) links
Immune system PDB id
2qqq
Jmol
Contents
Protein chains
109 a.a. *
Waters ×570
* Residue conservation analysis
PDB id:
2qqq
Name: Immune system
Title: Crystal structure of novel immune-type receptor 11 extracellular fragment from ictalurus punctatus
Structure: Novel immune-type receptor 11. Chain: a, b, c, d. Fragment: extracellular domain
Source: Ictalurus punctatus. Channel catfish
Resolution:
1.98Å     R-factor:   0.202     R-free:   0.259
Authors: D.A.Ostrov,J.A.Hernandez Prada,R.N.Haire,J.P.Cannon, A.T.Magis,K.M.Bailey,G.W.Litman
Key ref: J.P.Cannon et al. (2008). A bony fish immunological receptor of the NITR multigene family mediates allogeneic recognition. Immunity, 29, 228-237. PubMed id: 18674935
Date:
26-Jul-07     Release date:   10-Jun-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8UWK4  (Q8UWK4_ICTPU) -  Novel immune-type receptor 11
Seq:
Struc:
185 a.a.
109 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Immunity 29:228-237 (2008)
PubMed id: 18674935  
 
 
A bony fish immunological receptor of the NITR multigene family mediates allogeneic recognition.
J.P.Cannon, R.N.Haire, A.T.Magis, D.D.Eason, K.N.Winfrey, J.A.Hernandez Prada, K.M.Bailey, J.Jakoncic, G.W.Litman, D.A.Ostrov.
 
  ABSTRACT  
 
Novel immune-type receptors (NITRs) comprise an exceptionally large, diversified family of activating and inhibitory receptors that has been identified in bony fish. Here, we characterized the structure of an activating NITR that is expressed by a cytotoxic natural killer (NK)-like cell line and that specifically binds an allogeneic B cell target. A single amino acid residue within the NITR immunoglobulin variable (V)-type domain accounts for specificity of the interaction. Structures solved by X-ray crystallography revealed that the V-type domains of NITRs form homodimers resembling rearranging antigen-binding receptor heterodimers. CDR1 elements of both subunits of NITR dimers form ligand-binding surfaces that determine specificity for the nonself target. In the evolution of immune function, it appears that a specific NK type of innate recognition may be mediated by a complex germline multigene family of V structures resembling those that are somatically diversified in adaptive immunological responses.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21191578 J.A.Yoder, and G.W.Litman (2011).
The phylogenetic origins of natural killer receptors and recognition: relationships, possibilities, and realities.
  Immunogenetics, 63, 123-141.  
20651744 G.W.Litman, J.P.Rast, and S.D.Fugmann (2010).
The origins of vertebrate adaptive immunity.
  Nat Rev Immunol, 10, 543-553.  
20012603 J.A.Yoder, P.M.Turner, P.D.Wright, V.Wittamer, J.Y.Bertrand, D.Traver, and G.W.Litman (2010).
Developmental and tissue-specific expression of NITRs.
  Immunogenetics, 62, 117-122.  
20004115 J.P.Cannon, L.J.Dishaw, R.N.Haire, R.T.Litman, D.A.Ostrov, and G.W.Litman (2010).
Recognition of additional roles for immunoglobulin domains in immune function.
  Semin Immunol, 22, 17-24.  
19851764 S.Ferraresso, H.Kuhl, M.Milan, D.W.Ritchie, C.J.Secombes, R.Reinhardt, and L.Bargelloni (2009).
Identification and characterisation of a novel immune-type receptor (NITR) gene cluster in the European sea bass, Dicentrarchus labrax, reveals recurrent gene expansion and diversification by positive selection.
  Immunogenetics, 61, 773-788.  
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