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HLA-DM
HLA-DM (human leukocyte antigen DM) is an intracellular protein involved in the mechanism of antigen presentation on antigen presenting cells (APCs) of the immune system. It does this by assisting in peptide loading of major histocompatibility complex (MHC) class II membrane-bound proteins. HLA-DM is encoded by the genes HLA-DMA and HLA-DMB.
HLA-DM is a molecular chaperone that works in lysosomes and endosomes in cells of the immune system. It works in APCs like macrophages, dendritic cells, and B cells by interacting with MHC class II molecules. HLA-DM protects the MHC class II molecules from breaking down, and regulates which proteins or peptides bind to them as well. This regulates how and when a peptide acts as an antigen initiating an immune response. Thus, HLA-DM is necessary for the immune system to respond effectively to a foreign invader. Impairment in HLA-DM function can result in immunodeficiency and autoimmune diseases.
The genes for HLA-DM are located in the MHCII region of the human chromosome 6. The genes code for the alpha and beta chains that make up the protein.
The gene is nonpolymorphic.
HLA-DM is an integral protein in the mechanism regulating which antigens are presented extracellularly on APCs. It binds partially to the peptide-binding groove of MHC class II molecules. This can affect how well your immune system responds to foreign invaders.
HLA-DM is required to release CLIP from MHC class II molecules, to chaperone empty MHC molecules against denaturation, and to control proper loading and release of peptides at the peptide-binding groove. It also interacts heavily with chaperone protein HLA-DO. All of this ensures proper antigen presentation by an APC, to activate other immune cells. This is critical to rid the body of harmful infections. For example, proper antigen presentation benefits T cell activation, and memory T cell survival and generation. Without it, T cells leaving their site of production and entering the circulatory vessels of the body will not be activated against a danger. The immune system will not be able to kill dangerous or infected cells, and will not react quickly against a second infection.
The low pH of lysosomes could cause denaturation or proteolysis of MHC class II molecules. HLA-DM binding to MHC stabilizes and protects from degradation, by covering hydrophobic surfaces. Antigen degradation could also ensue, resulting in an inability to bind to the peptide-binding groove. Thus, HLA-DM is needed to protect proteins against the lysosomal environment.
In order to ensure that no false peptides bind to an MHC class II molecule, the peptide-binding groove is occupied by a protein called CLIP. Once a proper peptide is encountered, HLA-DM catalyzes the exchange of CLIP for an antigen peptide. Often, this peptide is retrieved directly from the B cell receptor which internalized it. Through expulsion of CLIP at the proper time, HLA-DM ensures that the correct antigen can bind to MHC molecules and prevent either from degrading.
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HLA-DM
HLA-DM (human leukocyte antigen DM) is an intracellular protein involved in the mechanism of antigen presentation on antigen presenting cells (APCs) of the immune system. It does this by assisting in peptide loading of major histocompatibility complex (MHC) class II membrane-bound proteins. HLA-DM is encoded by the genes HLA-DMA and HLA-DMB.
HLA-DM is a molecular chaperone that works in lysosomes and endosomes in cells of the immune system. It works in APCs like macrophages, dendritic cells, and B cells by interacting with MHC class II molecules. HLA-DM protects the MHC class II molecules from breaking down, and regulates which proteins or peptides bind to them as well. This regulates how and when a peptide acts as an antigen initiating an immune response. Thus, HLA-DM is necessary for the immune system to respond effectively to a foreign invader. Impairment in HLA-DM function can result in immunodeficiency and autoimmune diseases.
The genes for HLA-DM are located in the MHCII region of the human chromosome 6. The genes code for the alpha and beta chains that make up the protein.
The gene is nonpolymorphic.
HLA-DM is an integral protein in the mechanism regulating which antigens are presented extracellularly on APCs. It binds partially to the peptide-binding groove of MHC class II molecules. This can affect how well your immune system responds to foreign invaders.
HLA-DM is required to release CLIP from MHC class II molecules, to chaperone empty MHC molecules against denaturation, and to control proper loading and release of peptides at the peptide-binding groove. It also interacts heavily with chaperone protein HLA-DO. All of this ensures proper antigen presentation by an APC, to activate other immune cells. This is critical to rid the body of harmful infections. For example, proper antigen presentation benefits T cell activation, and memory T cell survival and generation. Without it, T cells leaving their site of production and entering the circulatory vessels of the body will not be activated against a danger. The immune system will not be able to kill dangerous or infected cells, and will not react quickly against a second infection.
The low pH of lysosomes could cause denaturation or proteolysis of MHC class II molecules. HLA-DM binding to MHC stabilizes and protects from degradation, by covering hydrophobic surfaces. Antigen degradation could also ensue, resulting in an inability to bind to the peptide-binding groove. Thus, HLA-DM is needed to protect proteins against the lysosomal environment.
In order to ensure that no false peptides bind to an MHC class II molecule, the peptide-binding groove is occupied by a protein called CLIP. Once a proper peptide is encountered, HLA-DM catalyzes the exchange of CLIP for an antigen peptide. Often, this peptide is retrieved directly from the B cell receptor which internalized it. Through expulsion of CLIP at the proper time, HLA-DM ensures that the correct antigen can bind to MHC molecules and prevent either from degrading.
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