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Image of CD4 co-receptor binding to MHC (Major Histocompatibility Complex) non-polymorphic region. In molecular biology, CD4 (cluster of differentiation 4) is a glycoprotein that serves as a co-receptor for the T-cell receptor (TCR). CD4 is found on the surface of immune cells such as helper T cells, monocytes, macrophages, and dendritic cells.
The CD family of co-receptors are a well-studied group of extracellular receptors found in immunological cells. [4] 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]
Gp120 binds to a CD4 and a co-receptor (CCR5 or CXCR4), found on susceptible cells such as Helper T cells and macrophages. [5] As a result, a cascade of conformational changes occurs in the gp120 and gp41 proteins. These conformational changes start with gp120 that rearranges to expose the binding sites for the coreceptors mentioned above.
HLA-A projected away from the cell surface and presenting a peptide sequence. The peptide-MHC complex presents a surface that looks like an altered self to the TCR. [11] The surface consisting of two α helices from the MHC and a bound peptide sequence is projected away from the host cell to the T cells, whose TCRs are projected away from the T cells towards the host cells.
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]
The CD nomenclature was proposed and established in the 1st International Workshop and Conference on Human Leukocyte Differentiation Antigens (HLDA), held in Paris in 1982. [4] [5] This system was intended for the classification of the many monoclonal antibodies (mAbs) generated by different laboratories around the world against epitopes on the surface molecules of leukocytes (white blood cells).
CEF 3 is a multi-process implementation based on the Chromium Content API and has performance similar to Google Chrome. [6] It uses asynchronous messaging to communicate between the main application process and one or more render processes ( Blink + V8 JavaScript engine).
The extracellular and transmembrane part of the coreceptor is from wild-type CD8 coreceptor, whereas the intracellular domain from CD4 coreceptor. [1] This model was created to examine role of coreceptor coupling to Lck (lymphocyte-specific protein tyrosine kinase) [1] as the CD4 and CD8 coreceptors have an Lck-binding site in their ...