Unlocking the Potential of PSTPIP1: A Potent Drug Target and Biomarker

Target Name: PSTPIP1

NCBI ID: G9051

PSTPIP1

Unlocking the Potential of PSTPIP1: A Potent Drug Target and Biomarker

Phosphatidylserine (PS) is a well-known phospholipid that plays a crucial role in various cellular processes, including cell signaling, protein transport, and membrane structure. It is also an essential component of the endoplasmic reticulum (ER) and plays a key role in the transport of proteins involved in intracellular signaling pathways. The phosphatidylserine (PS) phosphatase (PSP) is an enzyme that regulates the levels of PS in the ER. The protein encoded by the gene PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and psychiatric disorders.

In this article, we will explore the structure and function of PSTPIP1, its potential drug targets, and its potential as a biomarker for various diseases.

Structure and Function

PSTPIP1 is a 164-kDa protein that is expressed in various tissues, including brain, heart, and muscle. It is composed of 115 amino acid residues and has a calculated pI of 4.5. PSTPIP1 is a single-pass protein that uses ATP as a phosphate donor to regulate the activity of the catalytic active site.

The catalytic active site of PSTPIP1 consists of a parallel beta-sheet, which is flanked by alpha-helices on both sides. The sheet has three distinct regions: an N-terminal region that contains a conserved alkaline amino acid (Ala-29), a catalytic active site region that contains a single catalytic active site (Asp-30), and a C-terminal region that contains a conserved aspartic acid (Asn-34).

The N-terminal region of PSTPIP1 contains a conserved alkaline amino acid (Ala-29), which is known to play a critical role in protein stability and functions. Ala-29 can interact with various amino acids, including Glu-31 and Lys-33, which may contribute to its stability and functions.

The catalytic active site region of PSTPIP1 contains a single catalytic active site (Asp-30), which is known to be a critical region for protein-protein interactions and catalytic activity. The Asp-30 residue can interact with various amino acids, including Asn-34, which may contribute to its catalytic activity.

The C-terminal region of PSTPIP1 contains a conserved aspartic acid (Asn-34), which is known to play a critical role in protein stability and functions. Asn-34 can interact with various amino acids, including Glu-31 and Lys-33, which may contribute to its stability and functions.

Potential Drug Targets

PSTPIP1 has been identified as a potential drug target due to its various functions in cellular processes. One of its functions is the regulation of the levels of PS in the ER. PS is a crucial component of the endoplasmic reticulum (ER), and its levels are regulated by various enzymes, including PSTPIP1. Therefore, targeting PSTPIP1 may be an effective way to regulate PS levels and treat various diseases.

Another potential drug target for PSTPIP1 is its role in the regulation of cellular signaling pathways. PSTPIP1 has been shown to interact with various proteins involved in cellular signaling pathways, including T-cell signaling pathways, insulin signaling pathways, and neurotransmitter signaling pathways. Therefore, targeting PSTPIP1

Protein Name: Proline-serine-threonine Phosphatase Interacting Protein 1

Functions: Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils

The "PSTPIP1 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 PSTPIP1 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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