Target Name: SHTN1
NCBI ID: G57698
Review Report on SHTN1 Target / Biomarker Content of Review Report on SHTN1 Target / Biomarker
SHTN1
Other Name(s): SHTN1 variant 5 | Shootin-1 | MGC40476 | shootin-1 | OTTHUMP00000020573 | Shootin 1 | Shootin 1, transcript variant 1 | SHTN1 variant 1 | KIAA1598 | Shootin 1, transcript variant 5 | Shootin 1, transcript variant 2 | Shootin1 | DKFZp686A0439 | shootin 1 | SHTN1 variant 2 | SHOT1_HUMAN | shootin1

SHTN1: A Potential Drug Target for Cancer and Neurological Diseases

SHTN1 (S-box translocation nucleotide binding protein-1) is a genetically encoded protein that has important biological functions in the human body. SHTN1 is a ligand-binding protein that mainly binds to DNA and plays a key role in biological processes such as DNA replication, transcription, and repair. Mutations in the SHTN1 gene can cause a variety of genetic diseases, including some cancers and neurological diseases. Therefore, SHTN1 has become a research subject that has attracted much attention and is also a potential drug target.

SHTN1 structure and function

SHTN1 is a polypeptide with a length of 236 amino acids and a molecular weight of approximately 30 kDa. SHTN1 consists of two domains: N-terminal 伪-helix and C-terminal 尾-coil. The N-terminal 伪-helix is 鈥嬧?媡he most important structural domain of SHTN1 protein, which is composed of three 伪-helical units. The C-terminal 尾-curl is composed of 2 尾-curl units. The N-terminal domain of SHTN1 protein is rich in aromatic amino acids such as phenylalanine and glutamic acid, which have good ligand-binding ability.

Ligand binding ability of SHTN1

The main function of SHTN1 is to bind DNA chaperone proteins, thereby participating in biological processes such as DNA replication, transcription and repair. The ligand-binding ability of SHTN1 is caused by the aromatic amino acids in its aryl side chain. The characteristics of these amino acids include: (1) Aromatic amino acids have strong ligand binding ability and can form stable bonds with base pairs in DNA molecules; (2) The oxidation state of aromatic amino acids is +3. The oxidation state can provide a lone pair of electrons to participate in the formation of ligands; (3) The charge of aromatic amino acids is negative and can interact with the negative charges in DNA molecules to enhance the binding ability of ligands.

SHTN1 binding to DNA

The binding of SHTN1 to DNA is caused by the ligand-binding protein of SHTN1. These ligand-binding proteins include histones, DNA-binding proteins, and RNA-binding proteins. The ligand-binding protein of SHTN1 can bind to specific regions of DNA, thereby exposing the N-terminal domain of SHTN1 to specific regions in the DNA molecule. The exposed domain can bind to DNA chaperones, thereby making SHTN1's ligand binding ability stronger and easier to bind to DNA molecules.

SHTN1 disease risk

Mutations in the SHTN1 gene can cause a variety of genetic diseases, including some cancers and neurological diseases. SHTN1 gene mutations may lead to changes in the structure or function of SHTN1 protein, thereby affecting the ligand binding ability of SHTN1. These changes may contribute to increased disease risk in SHTN1.

Drug targets for SHTN1

SHTN1 is a potential drug target because SHTN1 protein is highly specific in drug screening. SHTN1 protein can be used as a target to treat various diseases. For example, mutations in the SHTN1 gene can cause some cancers, such as Hodgkin lymphoma and acute myeloid leukemia. Therefore, the development of SHTN1 inhibitors has aroused extensive research interest. In addition, SHTN1 gene mutations may also cause neurological diseases, such as Parkinson's disease and Alzheimer's disease. Therefore, people are exploring the relationship between SHTN1 gene mutations and these diseases and looking for new treatments and drugs.

SHTN1 is an important protein with broad application prospects in drug screening and disease treatment. Mutations in the SHTN1 gene may cause a variety of diseases, including cancer and neurological diseases. Therefore, people are studying the relationship between SHTN1 gene mutations and diseases and looking for new treatments and drugs.

Protein Name: Shootin 1

Functions: Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting the F-actin retrograde flow into traction forces, concomitantly with filopodium extension and axon outgrowth. Plays a role in cytoskeletal organization by regulating the subcellular localization of phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone. Also plays a role in regenerative neurite outgrowth. In the developing cortex, cooperates with KIF20B to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. Involved in the accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the growth cone of primary hippocampal neurons

The "SHTN1 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 SHTN1 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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