Target Name: MAGT1
NCBI ID: G84061
Review Report on MAGT1 Target / Biomarker Content of Review Report on MAGT1 Target / Biomarker
MAGT1
Other Name(s): bA217H1.1 | Oligosaccharyl transferase subunit MAGT1 | UNQ628/PRO1244 | MRX95 | Magnesium transporter protein 1 [Precursor] | oligosaccharyl transferase subunit MAGT1 | MAGT1_HUMAN | magnesium transporter 1 | PRO0756 | Magnesium transporter protein 1 (isoform 2) | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1 | FLJ14726 | implantation-associated protein | Magnesium transporter protein 1 | MAGT1 variant 2 | OTTHUMP00000062081 | IAG2 | SLC58A1 | PSEC0084 | dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1 | CDG1CC | OTTHUMP00000023589 | XMEN | OST3B | oligosaccharyltransferase 3 homolog B | IAP | Implantation-associated protein | RP11-217H1.1 | DKFZp564K142 | MagT1 | MGC64926 | Magnesium transporter 1, transcript variant 2

Understanding MAGT1: Unlocking Its Potential as A Drug Target

MAGT1 (bA217H1.1) is a protein that is expressed in various tissues of the body, including the brain, heart, and kidneys. It is a member of the G-protein-coupled receptor (GPCR) family, which is a large superfamily of transmembrane proteins that play a critical role in cellular signaling.

One of the unique features of MAGT1 is its ability to interact with several different GPCRs, including GPCR-A, GPCR-B, GPCR-C, and GPCR-D. This interactivity makes MAGT1 an attractive drug target, as it allows it to modulate the activity of a wide range of GPCRs, rather than just one specific receptor.

MAGT1 has been shown to play a role in several physiological processes in the body, including neuronal signaling, neurotransmitter release, and blood pressure regulation. It has also been implicated in several diseases, including hypertension, diabetes, and neurodegenerative disorders.

One of the key challenges in studying MAGT1 is its high degree of cross-reactivity, as MAGT1 has been shown to interact with multiple GPCRs. This makes it difficult to identify and modify the target of MAGT1 without also affecting other GPCRs.

To address this challenge, researchers have used a variety of techniques to identify potential binding sites within MAGT1. These techniques include biochemical assays, such as immunoprecipitation and protein-fragment complementation assays, as well as functional assays, such as yeast single cell assays and cell -based assays.

One of the most promising approaches to studying MAGT1 is the use of small molecule inhibitors. These inhibitors can be designed to specifically bind to MAGT1 and modulate its activity, allowing researchers to study its role in different physiological processes.

Despite the promising potential of small molecule inhibitors, there are still several challenges that must be addressed before they can be used effectively. First, the full extent of MAGT1's interactivity with GPCRs is not yet fully understood, which can make it difficult to identify effective inhibitors . Second, the high degree of cross-reactivity of MAGT1 can make it difficult to predict the effects of small molecules on its activity.

In addition to these challenges, there is also a need for better understanding of the underlying molecular mechanisms that regulate MAGT1. This can be achieved by studying the structure and function of MAGT1, as well as its interacting proteins.

Overall, MAGT1 is a drug target (or biomarker) that has the potential to revolutionize our understanding of cellular signaling and the development of new treatments for a wide range of diseases. Further research is needed to fully understand its role and to develop effective small molecule inhibitors.

Protein Name: Magnesium Transporter 1

Functions: Accessory component of the STT3B-containing form of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains (PubMed:31831667). Involved in N-glycosylation of STT3B-dependent substrates (PubMed:31831667). Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with TUSC3. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Has also oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition

The "MAGT1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about MAGT1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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