Leukocyte-associated Ig-like receptor-1 (LAIR-1) is an inhibitory receptor of the Ig superfamily that is structurally related to inhibitory members of KIR and ILT/CD85 families. It is expressed on immune cells, including NK cells, T cells, B cells, monocytes, immature neutrophils, dendritic cells and most thymocytes.The 253 amino acid (aa) type I transmembrane (TM) protein contains a 21 aa signal sequence, a 124 aa extracellular domain (ECD), a 20 aa TM domain and a 98 aa cytoplasmic domain. The ECD includes one C2-type Ig-like domain and two potential N-linked glycosylation sites. Tyrosine phosphorylation of two cytoplasmic ITIM motifs results in recruitment of phosphatases and down-regulation of signaling through activating receptors. LAIR1 shows high-affinity binding of collagens that results in inhibition of degranulation in a basophilic leukemia cell line.