A Promising Potential Drug Target: STT3B, a Source of Immunodominant MHC-Associated Peptides Homolog

Target Name: STT3B

NCBI ID: G201595

A Promising Potential Drug Target: STT3B, a Source of Immunodominant MHC-Associated Peptides Homolog

The immune system is a critical mechanism that protects the body against external threats, such as viruses, bacteria, and cancer cells. The major histocompatibility complex (MHC) is a key molecule that plays a crucial role in the immune response by presenting antigens to T-cells. MHC-associated peptides (MAPs) are short chains of amino acids that are derived from antigens and are involved in the presentation of these antigens to CD4+ T-cells. STT3B, a source of immunodominant MHC-associated peptides homolog, has been identified as a potential drug target or biomarker for several diseases, including cancer, autoimmune disorders, and neurodegenerative diseases.

STT3B: A MHC-Associated Peptide Homolog

STT3B is a non-coding RNA molecule that was identified as a potential drug target by researchers due to its unique structure and the presence of several conserved domains, including a potential N-terminal transmembrane domain, a unique RING-like domain, and a C-terminal T-cell receptor (TCR) alpha-like domain. In addition to these conserved domains, STT3B has a unique feature, known as a double-stranded RNA structure, which is composed of two interconnected strands that are held together by a disulfide bond.

The MHC-associated peptides (MAPs) are derived from antigens and are involved in the presentation of these antigens to CD4+ T-cells. MAPs are typically derived from the major histocompatibility complex (MHC) and are involved in the immune response by allowing antigens to be processed and loaded onto CD4+ T-cells. STT3B has been shown to be a source of MAPs and has been identified as a potential drug target due to its unique structure and the potential functions it may have.

Potential Functions of STT3B as a Drug Target

STT3B has been shown to play a role in several diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. In cancer, STT3B has been shown to be involved in the development and progression of several types of cancer, including breast cancer, lung cancer, and colon cancer. In addition to its role in cancer, STT3B has also been shown to be involved in the development and progression of autoimmune disorders, such as rheumatoid arthritis (9) and multiple sclerosis.

In autoimmune disorders, STT3B has been shown to regulate the immune response and contribute to the pathogenesis of these disorders. For example, STT3B has been shown to regulate the production of antibodies in response to antigens and to play a role in the regulation ofT-cell responses.

In neurodegenerative diseases, STT3B has been shown to be involved in the development and progression of several neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease.

Conclusion

STT3B is a unique and promising potential drug target due to its unique structure and the potential functions it may have in several diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. Further research is needed to fully understand the role of STT3B

Protein Name: STT3 Oligosaccharyltransferase Complex Catalytic Subunit B

Functions: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient post-translational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins. Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation. Mediates glycosylation of the disease variant AMYL-TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation (PubMed:19167329, PubMed:22607976)

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