>KIR2DL1 / CD158a Protein
KIR2DL1 / CD158a Protein
Kller cell immunoglobulin-like receptor, two domains, long cytoplasmic tail, 1
KIR2DL1 Protein, Recombinant
|Molecule||Species||Description //For Detailed Info. and Price------CLICK!||Cat. No|
|KIR2DL1||Human||KIR2DL1 / CD158a Protein,Recombinant||13145-H02H|
|KIR2DL1||Human||KIR2DL1 / CD158a Protein, Recombinant||13145-H08H|
KIR2DL1 Related Areas
KIR2DL1 Alternative Names
XXbac-BPG184J6.7, CD158A, KIR-K64, KIR221, NKAT, NKAT1, p58.1[Homo sapiens]
Killer cell immunoglobulin-like receptor 2DL1 or KIR2DL1 is an inhibitory natural Killer cell immunoglobulin-like receptor with two extracellular immunoglobulin domains. KIR2DL1 is a member of the Killer cell immunoglobulin-like receptor family whose members are classified by the number of the extracellular immunoglobulin domains and the length of the cytoplasm domain. KIR2DL1 is a transmembrane glycoprotein expressed by natural killer cells and subsets of T cells. KIR2DL1 down-regulates the cytotoxicity of NK cells upon recognition of specific class I major histocompatibility complex (MHC) molecules on target cells. It has been reported that the KIR2DL1 bound to its class I MHC ligand, HLA-Cw4. The KIR2DL1-HLA-Cw4 interface exhibits charge and shape complementarity. Specificity is mediated by a pocket in KIR2DL1 that hosts the Lys80 residue of HLA-Cw4. Many residues conserved in HLA-C and in KIR2DL receptors make different interactions in KIR2DL1-HLA-Cw4 and in a previously reported KIR2DL2-HLA-Cw3 complex. A dimeric aggregate of KIR-HLA-C complexes was observed in one KIR2DL1-HLA-Cw4 crystal.
KIR2DL1 Related Studies
- Fan QR, et al. (2001) Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1-HLA-Cw4 complex. Nature Immunology. 2: 452-60.
- Wagtmann N, et al. (1995) Molecular clones of the p58 NK cell receptor reveal immunoglobulin-related molecules with diversity in both the extra- and intracellular domains. Immunity. 2 (5): 439-49.
- Colonna M, et al. (1995) Cloning of immunoglobulin-superfamily members associated with HLA-C and HLA-B recognition by human natural killer cells. Science. 268 (5209): 405-8.