BRCA1: A Non-Coding RNA Molecule as A Potential Drug Target for Breast Cancer

Target Name: BARD1

NCBI ID: G580

BARD1

BRCA1: A Non-Coding RNA Molecule as A Potential Drug Target for Breast Cancer

BRCA1 (BRAF-associated RNA domain 1) is a non-coding RNA molecule that is highly expressed in various tissues, including breast tissue, and is associated with the breast cancer. The discovery of BRCA1 as a potential drug target has generated a lot of interest in the field of breast cancer treatment. This article will introduce relevant information about BRCA1, including its structure, function and possibility as a drug target.

structure

BRCA1 is a non-coding RNA molecule about 290 nucleotides in length, which was first discovered in 1990 by researchers at the Broad Institute in the United States. The molecule encodes an 11-amino-acid protein that has multiple functions within cells, including regulating RNA binding, DNA binding, and chromatin structure.

The secondary structure of BRCA1 is composed of two major 伪-helices and three 尾-coils. Its 伪-helix is 鈥嬧?媍omposed of three secondary structural units, each unit containing a core 伪-helical structure with an axially extending 尾-coil. This secondary structure is composed of three secondary structure units, each unit containing a core 伪-helical structure with an axially extending 尾-coil.

The secondary structure of BRCA1 is composed of two major 伪-helices and three 尾-coils. Its 伪-helix is 鈥嬧?媍omposed of three secondary structural units, each unit containing a core 伪-helical structure with an axially extending 尾-coil. This secondary structure is composed of three secondary structure units, each unit containing a core 伪-helical structure with an axially extending 尾-coil.

Function

BRCA1 has multiple functions in cells, including RNA binding, DNA binding, and chromatin structure. Research shows that BRCA1 can bind to multiple types of RNA, including mRNA, rRNA and hnRNA. It can also bind DNA and participate in DNA binding and chromatin structure.

The RNA-binding ability of BRCA1 is determined by its structure. The molecule contains an N-terminal 伪-helix and a C-terminal 尾-coil. The N-terminal alpha helix binds one type of RNA, while the C-terminal beta coil binds another type of RNA. This binding ability enables BRCA1 to selectively bind to mRNA and rRNA, thereby participating in gene expression and transcription.

The DNA-binding ability of BRCA1 is also determined by its structure. The molecule contains an N-terminal 伪-helix and two C-terminal 尾-coils. The N-terminal 伪-helix can bind to DNA, while the C-terminal 尾-coil can bind to the promoter region of DNA. This binding ability allows BRCA1 to selectively bind DNA and participate in gene expression and transcription.

The chromatin structural ability of BRCA1 is also determined by its structure. The molecule contains an N-terminal 伪-helix and two C-terminal 尾-coils. The N-terminal 伪-helix can bind to chromatin histones and thus participate in the structure of chromatin. The C-terminal 尾-coil binds to open chromatin complexes and participates in chromatin transcription.

as a drug target

As a non-coding RNA molecule, BRCA1 has a unique structure and therefore may be a potential drug target. Currently, a variety of drugs have been developed to treat BRCA1-related breast cancer, including anti-tumor drugs, anti-inflammatory drugs, and immunomodulatory drugs.

Among them, anti-tumor drugs are currently one of the most commonly used drugs. For example, osimertinib, an inhibitor of Brca1-associated protein (BAP), has been used to treat BRCA1-positive breast cancer. Studies have shown that osimertinib can significantly improve the progression-free survival and overall survival of patients with BRCA1-positive breast cancer, making it a potential breast cancer treatment drug.

In addition, anti-inflammatory drugs are also potential drug targets. For example, montelukast is an inhibitor of nuclear factor kappa B (NF

Protein Name: BRCA1 Associated RING Domain 1

Functions: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage

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