CD4 is an approximately 55 kDa type I membrane glycoprotein that is expressed predominantly on most thymocytes and a subset of mature T lymphocytes. In humans, CD4 is also expressed to a lesser extent on monocytes and macrophage related cells. Human CD4 cDNA encodes a 458 amino acid (aa) residue precursor protein with a 25 aa residue signal peptide, a 371 aa residue extracellular region containing four immunoglobulin homology domains, a 24 aa residue transmembrane domain and a 38 aa residue cytoplasmic domain.
CD4, also known as T4/Leu-3, is a 55 kD single-chain type I transmembrane glycoprotein and member of the immunoglobulin superfamily. It is expressed on most thymocytes, helper T cells, type II NKT cells, and monocytes/macrophages. CD4 is part of the TCR/CD3 complex, binds to β2 domain from the MHC class II molecule, and participates in TCR signal transduction. CD4 is the receptor of IL-16 and is a coreceptor for the human immunodeficiency virus (HIV) and human herpes virus 7 (HHV-7).
CD58, also known as lymphocyte function-associated antigen 3 (LFA-3) is a 45-70 kD cell surface protein that is a member of the immunoglobulin superfamily. Alternative splicing of CD58 gives rise to transmembrane and glycosylphosphatidylinositol (GPI)-anchored forms on cell surface. CD58 is expressed on both hematopoietic and non-hematopoietic cells including B cells, T cells, monocytes, erythrocytes, endothelial cells, epithelial cells, and fibroblasts. High levels are observed on memory T cells and dendritic cells. CD58 expressed on antigen presenting cells and target cells enhances T cell recognition via the binding of it's cognate ligand, CD2, on the T cell surface.
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