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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.
As well as being involved in forming a complex with MHC-II with TCR to control T-cell fate, the CD4 receptor is infamously the primary receptor that HIV envelope glycoprotein GP120 binds to. [6] In comparison, CD28 acts as a ‘co-coreceptor’ (costimulatory receptor) for the MHC-II binding with TCR and CD4. CD28 increases the IL-2 secretion ...
CD4-Ig works by mimicking the binding of CD4 to HIV, thereby preventing the virus from infecting T-helper cells. HIV infects T-helper cells by binding to the CD4 receptor and the co-receptor CCR5 or CXCR4. CD4-Ig binds to the viral envelope glycoprotein gp120, which is responsible for HIV binding to CD4. By binding to gp120, CD4-Ig prevents the ...
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).
The binding of CD154 on T H cells to CD40 activates antigen presenting cells and induces a variety of downstream effects. Activated CD4+ T cells primarily exhibit its ligand CD40L/CD154 to antigen-presenting cells including dendritic cells (DCs), B cells, macrophages, classical and non-classical monocytes, on a variety of non-immune cells ...
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.
The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, [1] [2] consisting of about 125 amino acids.
CD4 binding site: CDRH3 loop: b12: 1991 CDRH3 loop: HJ16: 2010 CDRH3 loop: CH103–106: 2013 Mimics CD4 via CDRH2: VRC01–03: 2010 Mimics CD4 via CDRH2: VRC-PG04, 04b: 2011 Mimics CD4 via CDRH2: VRC-CH30–34: 2011 Mimics CD4 via CDRH2: 3BNC117, 3BNC60: 2011 Mimics CD4 via CDRH2: NIH45–46: 2011 Mimics CD4 via CDRH2: 12A12, 12A21: 2011 Mimics ...