NKp30 as a mediator of NK activity

The structure of NKp30

The work of Pende and co-workers, in which NKp30 was first identified, demonstrated the importance of this receptor in the lysis of several tumour cell lines (Pende et al., 1999). More recently, its structure has been obtained by X-ray crystallography, revealing features distinct from the other known NCRs (Joyce, Tran, Zhuravleva, Jaw, Colonna & Sun, 2011).
The ectodomain of NKp30 contains an immunoglobulin (Ig)-like fold, connected to a transmembrane α-helix via a short stalk domain. The Ig-like domain is comprised of eight β-strands, forming two antiparallel β-sheets, linked by a disulphide bond between Cys39 and Cys108 (Figure 3 )(Joyce, Tran, Zhuravleva, Jaw, Colonna & Sun, 2011; Li, Wang & Mariuzza, 2011; Pende et al., 1999).