Target Name: HSPBP1
NCBI ID: G23640
Review Report on HSPBP1 Target / Biomarker Content of Review Report on HSPBP1 Target / Biomarker
HSPBP1
Other Name(s): Hsp70-binding protein 1 | Hsp70-interacting protein 2 | Hsp70-interacting protein 1 | HspBP1 | Hsp70 binding protein 1 | heat shock protein-binding protein 1 | HSPBP1 variant 1 | HspBP2 | Heat shock protein-binding protein 1 | HSPBP | Hsp70-binding protein 1 (isoform 2) | Hsp70-binding protein 2 | FES1 | hsp70 interacting protein | HSPA (Hsp70) binding protein 1, transcript variant 1 | HSPA (heat shock 70kDa) binding protein, cytoplasmic cochaperone 1 | Hsp70 interacting protein | HPBP1_HUMAN | HSPA (Hsp70) binding protein 1

HSPBP1: A Potential Drug Target and Biomarker

Hsp70 ( heat shock protein 70) is a family of proteins that play a crucial role in the regulation of various cellular processes, including stress response, DNA damage repair, and inflammation. Hsp70 proteins have been identified as potential drug targets due to their ability to interact with a variety of small molecules, including drugs, toxins, and other substances that can modulate their activity. One of the well-known Hsp70 proteins is HSPBP1 (Hsp70-binding protein 1), which is a protein that interacts with Hsp70 proteins. In this article, we will discuss the potential drug target of HSPBP1 and its potential as a biomarker.

The HSPBP1 Protein

HSPBP1 is a protein that is expressed in a variety of tissues, including the brain, heart, liver, and kidneys. It is a 21-kDa protein that contains a unique N-terminal region that is known as the HSPBP1-N-terminal domain. This domain is rich in acidic and basic residues, which give it a pKa of 6.8 and a charge of +2, making it an electrostatic attractor. This is why HSPBP1 is often called an electrostatic interactor.

The HSPBP1-N-terminal domain is responsible for the protein's ability to interact with Hsp70 proteins. Hsp70 proteins are known for their ability to form a stable complex with other molecules, including small molecules, peptides, and even entire proteins. This interaction between Hsp70 proteins and other molecules is critical for their proper function, and it is through this interaction that HSPBP1 plays its role.

HSPBP1's Interaction with Hsp70 Proteins

HSPBP1 has been shown to interact with a variety of Hsp70 proteins, including HSPB10, HSPB11, HSPB12, HSPB13, HSPB14, HSPB15, HSPB16, HSPB17, HSPB18, HSPB19, HSPB20, HSPB21, HSPB22, HSPB23, HSPB24, HSPB25, and HSPB26. These interactions have been shown to modulate the activity of these Hsp70 proteins, including their stability, activity, and sensitivity to various conditions, such as stress, temperature, and pH.

One of the most significant interactions between HSPBP1 and Hsp70 protein is the one between HSPBP1 and HSPB10. HSPBP1 has been shown to form a stable complex with HSPB10, which is known as the HSPBP1-HSPB10 complex. This complex has been shown to play a role in stress response, DNA damage repair, and inflammation.

Another interaction between HSPBP1 and Hsp70 protein is the one between HSPBP1 and HSPB13. HSPBP1 has been shown to form a stable complex with HSPB13, which is known as the HSPBP1-HSPB13 complex. This complex has been shown to play a role in cell signaling and inflammation.

HSPBP1's Potential as a Drug Target

The potential drug target of HSPBP1 is based on its ability to interact with Hsp70 proteins. Drugs that can modulate the activity of Hsp70 proteins, such as inhibitors of the HSPBP1-HSPB10 complex or the HSPBP1-HSPB13 complex, could potentially be used to treat a variety of diseases.

For example, HSPBP1 has been shown to be involved in

Protein Name: HSPA (Hsp70) Binding Protein 1

Functions: Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR

The "HSPBP1 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 HSPBP1 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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