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2QTE

Crystal Structure of Novel Immune-Type Receptor 11 Extracellular Fragment Mutant N30D

Summary for 2QTE
Entry DOI10.2210/pdb2qte/pdb
Related2QHL 2QJD 2QQQ
DescriptorNovel immune-type receptor 11 (2 entities in total)
Functional Keywordsimmunoglobulin variable domain-like beta-sandwich, immune-type receptor, immune system
Biological sourceIctalurus punctatus
Total number of polymer chains4
Total formula weight51373.92
Authors
Ostrov, D.A.,Hernandez Prada, J.A.,Haire, R.N.,Cannon, J.P.,Magis, A.T.,Bailey, K.M.,Litman, G.W. (deposition date: 2007-08-01, release date: 2008-09-02, Last modification date: 2024-10-30)
Primary citationCannon, J.P.,Haire, R.N.,Magis, A.T.,Eason, D.D.,Winfrey, K.N.,Hernandez Prada, J.A.,Bailey, K.M.,Jakoncic, J.,Litman, G.W.,Ostrov, D.A.
A bony fish immunological receptor of the NITR multigene family mediates allogeneic recognition.
Immunity, 29:228-237, 2008
Cited by
PubMed 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.
PubMed: 18674935
DOI: 10.1016/j.immuni.2008.05.018
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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数据于2024-11-06公开中

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