LIG4: A Negatively ChargedIg with Multiple Functions in Biology

Target Name: LIG4

NCBI ID: G3981

LIG4

LIG4: A Negatively ChargedIg with Multiple Functions in Biology

LIG4 (DNLI4_HUMAN) is a protein that is expressed in various tissues throughout the body, including the lungs, heart, kidneys, and intestines. It is a member of the immune globulin superfamily, belongs to the IG superfamily, and has important roles in biomedical research important biological significance.

LIG4 is a negatively charged immunoglobulin with a molecular weight of 28.5 kDa. It consists of two subunits, each with a molecular weight of 14.7 kDa. The subunits of LIG4 include 伪 and 尾 subunits, which are linked together by disulfide bonds.

LIG4 has multiple functions in biology. For example, it can act as an immune system suppressant, thereby preventing the immune system from overreacting. LIG4 can also serve as an indicator of inflammatory responses because it can be activated and induce cells to produce inflammatory factors.

In addition, LIG4 is also closely related to the occurrence and development of various diseases. For example, studies have shown that LIG4 expression levels can be used to predict survival in renal failure and also serve as a potential biomarker for liver cirrhosis.

LIG4 is also a new class of drug target. For example, researchers have discovered compounds called LIG4 inhibitors that inhibit the activation of LIG4 and dampen the inflammatory response. This compound has been used to treat a variety of conditions, including inflammatory arthritis and autoimmune diseases.

In addition, LIG4 is also closely related to the occurrence and development of tumors. Studies have shown that the expression level of LIG4 can be used to predict tumor invasion and metastasis, thereby helping doctors develop more effective treatment plans.

Overall, LIG4 is a very important protein that is of great significance in both biological research and medical practice. With the deepening of research, LIG4 is expected to become a new class of drug target and provide new solutions for the treatment of various diseases.

Protein Name: DNA Ligase 4

Functions: DNA ligase involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair and V(D)J recombination (PubMed:8798671, PubMed:9242410, PubMed:9809069, PubMed:12517771, PubMed:17290226). Catalyzes the NHEJ ligation step of the broken DNA during DSB repair by resealing the DNA breaks after the gap filling is completed (PubMed:9242410, PubMed:9809069, PubMed:12517771, PubMed:17290226). Joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction (PubMed:9242410, PubMed:9809069, PubMed:12517771, PubMed:17290226). LIG4 is mechanistically flexible: it can ligate nicks as well as compatible DNA overhangs alone, while in the presence of XRCC4, it can ligate ends with 2-nucleotides (nt) microhomology and 1-nt gaps (PubMed:17290226). Forms a subcomplex with XRCC4; the LIG4-XRCC4 subcomplex is responsible for the NHEJ ligation step and XRCC4 enhances the joining activity of LIG4 (PubMed:9242410, PubMed:9809069). Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends (PubMed:10854421). LIG4 regulates nuclear localization of XRCC4 (PubMed:24984242)

The "LIG4 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 LIG4 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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