The Structure of the Atypical Killer Cell Immunoglobulin-like Receptor, KIR2DL4
Shoeib Moradi, Richard Berry, Phillip Pymm, Corinne Hitchen, Simone A Beckham, Matthew CJ Wilce, Nicholas G Walpole, Craig S Clements, Hugh H Reid, Matthew A Perugini, Andrew G Brooks, Jamie Rossjohn, Julian P Vivian
JOURNAL OF BIOLOGICAL CHEMISTRY | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2015
The engagement of natural killer cell immunoglobulin-like receptors (KIRs) with their target ligands, human leukocyte antigen (HLA) molecules, is a critical component of innate immunity. Structurally, KIRs typically have either two (D1-D2) or three (D0-D1-D2) extracellular immunoglobulin domains, with the D1 and D2 domain recognizing the α1 and α2 helices of HLA, respectively, whereas the D0 domain of the KIR3DLs binds a loop region flanking the α1 helix of the HLA molecule. KIR2DL4 is distinct from other KIRs (except KIR2DL5) in that it does not contain a D1 domain and instead has a D0-D2 arrangement. Functionally, KIR2DL4 is also atypical in that, unlike all other KIRs, KIR2DL4 has both ac..View full abstract
Awarded by Australian Research Council (ARC)
Awarded by National Health and Medical Research Council (NHMRC) of Australia
Awarded by NHMRC Peter Doherty Fellowship
This work was supported by Australian Research Council (ARC) Grant DE130101504 and by National Health and Medical Research Council (NHMRC) of Australia Grant 1046685.Supported by NHMRC Peter Doherty Fellowship GNT1035636.Supported by an NHMRC Australia Fellowship. To whom correspondence may be addressed. E-mail: Jamie.email@example.com.Supported by an ARC DECRA Fellowship. To whom correspondence may be addressed. E-mail: Julian.firstname.lastname@example.org.