CD38, also called ADP-ribosyl cyclase, is a Type II integral membrane protein with 301 amino acids in length that belongs to the ADP-ribosyl cyclase family.It synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. And also moonlights as a receptor in cells of the immune system. CD38 is expressed in B and T lymphocytes, osteoclasts, and in cardiac, pancreatic, liver and kidney cells. Through its production of cyclic ADP-ribose, CD38 modulates calcium-mediated signal transduction in many types of cells, including neutrophils and pancreatic beta cells.
T-cell surface glycoprotein CD3 delta chain (CD3D) is a single-pass type I membrane protein. CD3D, together with CD3-gamma, CD3-epsilon and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. CD3 chains are present as CD3gammaepsilon, deltaepsilon, and zetazeta dimers in the receptor complex and play critical roles in the antigen receptor assembly, transport to the cell surface, and the receptor-mediated signal transduction. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. The T cell receptor-CD3 complex is unique in having ten cytoplasmic immunoreceptor tyrosine-based activation motifs(ITAMs). CD3D contains 1 ITAM domain and has been shown to interact with CD8A.
T-cell surface glycoprotein CD3D & CD3E, also known as CD3 delta & CD3 epsilon chain, are single-pass type I membrane proteins. CD3D, together with CD3- epsilon(CD3E) , CD3-gamma and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways.
T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.
CD40 is a Type I Transmembrane Glycoprotein that belongs to the TNF Receptor Superfamily. CD40 is expressed in B cells, follicular dendritic cells, dendritic cells, activated monocytes, macrophages, endothelial cells, vascular smooth muscle cells, and several tumor cell lines. The extracellular domain of CD40 is characterized by Cysteine rich repeat regions. Interaction of CD40 with its ligand (CD40L) leads to aggregation of CD40 molecules, which in turn interact with cytoplasmic components to initiate signaling pathways. Several different TRAF proteins (adaptor proteins) have been identified to serves as mediators of the signal transduction.
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