CD48 (also known as Blast-1 or SLAMF2) is a coactivator and adhesion molecule on cells with a hematopoietic origin []. It contains a glycosylphosphatidylinositol membrane anchor and can serve as a receptor for SLAMF4 (also known as CD244) []. It regulates adaptive immune responses by providing longer access of putative antigen presenting cells to virus-specific effector T cells by prolonging the time frame of effective stimulation [].
2B4 is a transmembrane receptor which is expressed primarily on natural killer (NK) cells. It plays a role in activating NK-mediated cytotoxicity through its interaction with CD48 on target cells in a subset of CD8 T cells []. The structure of 2B4 consists of an immunoglobulin variable domain fold and contains two β-sheets. One of the β-sheets, the six-stranded sheet, contains structural features that may have a role in ligand recognition and receptor function [].This entry represents the 2B4 immunoglobulin domain.
2B4 is a transmembrane receptor which is expressed primarily on natural killer (NK) cells. It plays a role in activating NK-mediated cytotoxicity through its interaction with CD48 on target cells in a subset of CD8 T cells []. The structure of 2B4 consists of an immunoglobulin variable domain fold and contains two β-sheets. One of the β-sheets, the six-stranded sheet, contains structural features that may have a role in ligand recognition and receptor function [].
The CD2 adhesion molecule is a cell surface protein expressed by T cells and natural killer cells. CD2's extracellular domain contains immunoglobulin-like domains that are glycosylated at two sites and can mediate homodimerisation []. Ligation of CD2 by CD58 in humans or CD48 in mice helps T cells adhere to antigen-presenting cells, and initiates signal transduction pathways that enhance signalling through the T cell receptor for antigen. CD2 knockout mice exhibit essentially normal immune function [], and it is thought that CD2 is somewhat functionally redundant with other T cell co-stimulatory receptors such as CD28 [].
The LFA-3 (CD2) adhesion molecule is a cell surface protein expressed by T cells and natural killer cells. LFA-3's extracellular region contains immunoglobulin-like domains that are glycosylated at two sites and can mediate homodimerisation []. Ligation of LFA3 by CD58 in humans or CD48 in mice helps T cells adhere to antigen-presenting cells, and initiates signal transduction pathways that enhance signalling through the T cell receptor for antigen. LFA-3 knockout mice exhibit essentially normal immune function [], and it is thought that LFA-3 is somewhat functionally redundant with other T cell co-stimulatory receptors such as CD28 [].
