2QTE

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

2QTE の概要

• エントリーDOI: 10.2210/pdb2qte/pdb
• 関連するPDBエントリー: 2QHL 2QJD 2QQQ
• 分子名称: Novel immune-type receptor 11 (2 entities in total)
• 機能のキーワード: immunoglobulin variable domain-like beta-sandwich, immune-type receptor, immune system
• 由来する生物種: Ictalurus punctatus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51373.92

構造登録者

Ostrov, D.A.,Hernandez Prada, J.A.,Haire, R.N.,Cannon, J.P.,Magis, A.T.,Bailey, K.M.,Litman, G.W. (登録日: 2007-08-01, 公開日: 2008-09-02, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)