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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.
The binding of the antigen-MHC to the TCR complex and CD4 may also help the APC and the T h cell adhere during T h cell activation, but the integrin protein LFA-1 on the T cell and ICAM on the APC are the primary molecules of adhesion in this cell interaction.
Complement component 4 (C4), in humans, is a protein involved in the intricate complement system, originating from the human leukocyte antigen (HLA) system. It serves a number of critical functions in immunity, tolerance, and autoimmunity with the other numerous components.
959 21947 Ensembl ENSG00000102245 ENSMUSG00000031132 UniProt P29965 P27548 RefSeq (mRNA) NM_000074 NM_011616 RefSeq (protein) NP_000065 NP_035746 Location (UCSC) Chr X: 136.65 – 136.66 Mb Chr X: 56.26 – 56.27 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse CD154, also called CD40 ligand or CD40L, is a protein that is primarily expressed on activated T cells and is a member of the ...
CTLA-4 is a member of the immunoglobulin superfamily that is expressed by activated T cells and transmits an inhibitory signal to T cells.CTLA-4 is homologous to the T-cell co-stimulatory protein, CD28, and both molecules bind to CD80 and CD86, also called B7-1 and B7-2 respectively, on antigen-presenting 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 α1 and β1 regions of the chains come together to make a membrane-distal peptide-binding domain, while the α2 and β2 regions, the remaining extracellular parts of the chains, form a membrane-proximal immunoglobulin-like domain. The antigen binding groove, where the antigen or peptide binds, is made up of two α-helixes walls and β-sheet ...
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]