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PDBsum entry 3b5t
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Immune system receptor
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PDB id
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3b5t
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Immune system receptor
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Title:
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Crystal structure of novel immune-type receptor 10 se-met extracellular fragment mutant n30d
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Structure:
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Novel immune-type receptor 10. Chain: a, b, c, d, e. Fragment: extracellular fragment. Engineered: yes. Mutation: yes
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Source:
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Ictalurus punctatus. Channel catfish. Organism_taxid: 7998. Gene: nitr10. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.75Å
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R-factor:
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0.185
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R-free:
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0.217
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Authors:
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D.A.Ostrov,J.A.Hernandez Prada,R.N.Haire,J.P.Cannon,A.T.Magis, K.M.Bailey,G.W.Litman
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Key ref:
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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:
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Date:
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26-Oct-07
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Release date:
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24-Jun-08
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PROCHECK
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Headers
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References
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Q8UWK5
(Q8UWK5_ICTPU) -
Novel immune-type receptor 10 from Ictalurus punctatus
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Seq:
Struc:
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206 a.a.
109 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Immunity
29:228-237
(2008)
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PubMed id:
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A bony fish immunological receptor of the NITR multigene family mediates allogeneic recognition.
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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.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.A.Yoder,
and
G.W.Litman
(2011).
The phylogenetic origins of natural killer receptors and recognition: relationships, possibilities, and realities.
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Immunogenetics,
63,
123-141.
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G.W.Litman,
J.P.Rast,
and
S.D.Fugmann
(2010).
The origins of vertebrate adaptive immunity.
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Nat Rev Immunol,
10,
543-553.
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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.
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Immunogenetics,
62,
117-122.
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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.
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Semin Immunol,
22,
17-24.
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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.
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Immunogenetics,
61,
773-788.
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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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Links
