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CD4 is a co-receptor of the T cell receptor (TCR) and assists the latter in communicating with antigen-presenting cells. The TCR complex and CD4 bind to distinct regions of the antigen-presenting MHC class II molecule. The extracellular D 1 domain of CD4 binds to the β2 region of MHC class II.
CD4 immunoadhesin was first developed in the mid-1990s as a potential therapeutic agent and treatment for HIV/AIDS. The protein is a fusion of the extracellular domain of the CD4 receptor and the Fc domain of human immunoglobulin G (IgG), the most abundant antibody isotype in the human body. [1]
CD4 + T cells are generally treated as having a pre-defined role as helper T cells within the immune system. For example, when an antigen-presenting cell displays a peptide antigen on MHC class II proteins, a CD4 + cell will aid those cells through a combination of cell to cell interactions (e.g. CD40 (protein) and CD40L) and through cytokines.
The CD receptor family typically act as co-receptors, illustrated by the classic example of CD4 acting as a co-receptor to the T cell receptor (TCR) to bind major histocompatibility complex II (MHC-II). [5] This binding is particularly well-studied in T-cells where it serves to activate T-cells that are in their resting (or dormant) phase and ...
Each B cell and T cell is specific for a particular antigen, which simply means that each of these cells is able to bind to a particular molecular structure (such as an antigen). The specificity of binding resides in a specific receptor for antigen: the B-cell receptor (BCR) and the T-cell receptor (TCR) for B and T cells, respectively. Both ...
It delivers cytosolic peptides into the endoplasmic reticulum (ER), where they bind to nascent MHC class I molecules. [2] The TAP structure is formed of two proteins: TAP-1 and TAP-2, which have one hydrophobic region and one ATP-binding region each. They assemble into a heterodimer, which results in a four-domain transporter.
CD86 and CD80 bind as ligands to costimulatory molecule CD28 on the surface of all naïve T cells, [17] and to the inhibitory receptor CTLA-4 (cytotoxic T-lymphocyte antigen-4, also known as CD152). [ 18 ] [ 19 ] CD28 and CTLA-4 have important, but opposite roles in the stimulation of T cells.
The motif contains a tyrosine separated from a leucine or isoleucine by any two other amino acids, giving the signature YxxL/I. [1] Two of these signatures are typically separated by between 6 and 8 amino acids in the cytoplasmic tail of the molecule (YxxL/Ix (6-8) YxxL/I). However, in various sources, this consensus sequence differs, mainly in ...