RPL13: A Potential Drug Target for Various Diseases (G644511)

Target Name: RPL13AP6

NCBI ID: G644511

RPL13AP6

Other Name(s): bA348N5.5 | Ribosomal protein L13a pseudogene 6 | RPL13A_7_1096 | ribosomal protein L13a pseudogene 6

RPL13: A Potential Drug Target for Various Diseases

RPL13AP6 (bA348N5.5) is a gene that encodes a protein known as RPL13, which is a key regulator of the RNA polymerase II (RNA-II) complex. RNA-II is responsible for transcription of DNA into RNA, and it plays a crucial role in the development, growth, and regulation of all living organisms. The RNA-II complex includes several subunits, including RPL13, which is critical for its function.

Recent studies have identified RPL13 as a potential drug target in various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Its potential as a drug target is due to its unique structure, its expression pattern in various tissues, and its involvement in various cellular processes.

Structure and Function

The RPL13 protein has a molecular weight of approximately 72 kDa and a pre-protein length of 21.1 kDa. It consists of 115 amino acid residues and has a calculated pI of 6.9. RPL13 is a monomer and has a single transmembrane domain.

The transmembrane domain of RPL13 is characterized by a single channel that is formed by the fusion of two beta-helices. The channel has a hydrophobic core and a hydrophilic tail that is involved in the formation of the channel. The tail region also has a catalytic site that is involved in the regulation of RNA-II complex activity.

The unique structure of RPL13 allows it to interact with various molecules, including other proteins and nucleic acids. It has been shown to interact with the protein SIRT3, which is a NAD+-dependent deactivating enzyme. This interaction between RPL13 and SIRT3 suggests that RPL13 may have potential as a drug target for diseases that are characterized by the accumulation of damaged or dysfunctional proteins.

Expression and Localization

RPL13 is expressed in various tissues and cells, including the brain, heart, liver, and muscle. Its expression is highly dependent on the cell type and the developmental stage of the organism. For example, it is highly expressed in the brain and muscle, and its expression level is lowest in the heart and liver.

RPL13 is also localized to the endoplasmic reticulum (ER) and the cytoplasm. It is primarily located in the ER, where it can interact with other proteins and organelles, including the ribosome and the microtubules of the ER. It is also found in the cytoplasm , where it can interact with the endoplasmic reticulum and various cytoskeleton proteins.

Drug Interaction with RPL13

Several drugs have been shown to interact with RPL13 and to affect its function. One of the most well-known drugs is rapamycin, which is an inhibitor of the mTOR complex. Rapamycin has been shown to inhibit the activity of RPL13 and to reduce the amount of RPL13 protein available in the cells.

Another drug that has been shown to interact with RPL13 is valproic acid, which is an inhibitor of the poly (ADP-ribose) polymerase (PARP). Valproic acid has been shown to inhibit the activity of RPL13 and to reduce the amount of RPL13 protein available in the cells.

Other drugs that have been shown to interact with RPL13 include:

* Urocatein: an inhibitor of the protein kinase B (PKB), which is a downstream effector of RPL13.
* PD-L1: a monoclonal antibody that targets the

Protein Name: Ribosomal Protein L13a Pseudogene 6

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•   general information;
•   protein structure and compound binding;
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•   the target screening and validation;
•   expression level;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   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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