PDBsum entry 3b5t

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Immune system receptor PDB id
Protein chains
109 a.a. *
Waters ×805
* Residue conservation analysis
PDB id:
Name: Immune system receptor
Title: Crystal structure of novel immune-type receptor 10 se-met extracellular fragment mutant n30d
Structure: Novel immune-type receptor 10. Chain: a, b, c, d, e. Fragment: extracellular fragment. Engineered: yes. Mutation: yes
Source: Ictalurus punctatus. Channel catfish. Organism_taxid: 7998. Gene: nitr10. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.75Å     R-factor:   0.185     R-free:   0.217
Authors: D.A.Ostrov,J.A.Hernandez Prada,R.N.Haire,J.P.Cannon,A.T.Magi 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
26-Oct-07     Release date:   24-Jun-08    
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Protein chains
Pfam   ArchSchema ?
Q8UWK5  (Q8UWK5_ICTPU) -  Novel immune-type receptor 10
206 a.a.
109 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)


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.
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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