3B5T

Crystal Structure of Novel Immune-Type Receptor 10 Se-Met Extracellular Fragment Mutant N30D

Summary for 3B5T

• Entry DOI: 10.2210/pdb3b5t/pdb
• Related: 2QHL 2QJD 2QQQ 2QTE
• Descriptor: Novel immune-type receptor 10 (2 entities in total)
• Functional Keywords: immunoglobulin variable domain-like beta-sandwich, immune-type receptor, immune system, immune system receptor
• Biological source: Ictalurus punctatus (Channel catfish)
• Total number of polymer chains: 5
• Total formula weight: 65465.65

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: 2007-10-26, release date: 2008-06-24, Last modification date: 2024-10-16)

Primary citation

Cannon, 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

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

Experimental method

X-RAY DIFFRACTION (1.75 Å)