Unlocking the Potential of VPS26C: A Drug Target and Biomarker for DSCR3 Arrestin Fold-Containing Structures

Target Name: VPS26C

NCBI ID: G10311

VPS26C

Unlocking the Potential of VPS26C: A Drug Target and Biomarker for DSCR3 Arrestin Fold-Containing Structures

Introduction

The protein domain containing a variable region (VPS26C) has been identified as a potential drug target and biomarker for diseases associated with disruptions in protein structure and function, including diseases caused by abnormalities in the structure of the protein involved. The DSCR3 (DNA-binding protein) arrestin fold, a conserved protein structure that plays a critical role in regulating DNA-protein interactions, has been identified as a potential target for VPS26C.

In this article, we will explore the structure and function of VPS26C and its potential as a drug target and biomarker. We will discuss the implications of the identification of VPS26C as a potential drug target and the potential for the development of new diagnostics and therapies based on this discovery.

Structure and Function of VPS26C

VPS26C is a 26 kDa protein that contains a unique variable region that includes a conserved N-terminal region, a unique C-terminal region, and a variable middle region. The middle region of VPS26C is rich in multiple conserved secondary structure elements, including a ??-sheet, a ??-strand, and a ??-sheet, which are believed to play a key role in the protein's stability and function.

One of the most striking features of VPS26C is its ability to form a stable complex with the protein DSCR3, a critical regulator of DNA-protein interactions. The DSCR3 protein forms a ??-sheet-??-sheet sandwich around the VPS26C protein, with the ??-sheet in the N-region and the ??-sheet in the C-region. This ??-sheet-??-sheet structure is held together by a unique interaction between the N-terminal and C-terminal regions of the protein.

The unique structure of VPS26C and its interaction with DSCR3 make it an attractive target for drug development. The potential drug targets for VPS26C include inhibitors of DNA-protein interactions, which may disrupt the stability and function of the protein, as well as antibodies that specifically target the protein and prevent its formation of the ??-sheet-??-sheet sandwich with DSCR3.

Potential as a Drug Target

The identification of VPS26C as a potential drug target has significant implications for the development of new treatments for diseases associated with disruptions in protein structure and function. The ability of VPS26C to form a stable complex with DSCR3 and the conservation of the ??-sheet-?? -sheet structure in the protein make it an attractive target for small molecules and antibodies that can disrupt the protein's stability and function.

One potential approach to targeting VPS26C is the use of small molecules that can disrupt the ??-sheet-??-sheet interaction with DSCR3. Small molecules that are able to bind specifically to the ??-sheet region of VPS26C and prevent its formation of the ?? -sheet-??-sheet sandwich with DSCR3 could be developed as potential drugs for the treatment of diseases associated with disruptions in protein structure and function.

In addition to small molecules, antibodies that specifically target VPS26C and prevent its formation of the ??-sheet-??-sheet sandwich with DSCR3 could also be developed as potential drugs. These antibodies would likely be derived from mice or other animals and be able to cross-react with a variety of different VPS26C isoforms.

Potential as a Biomarker

The identification of VPS26C as a potential drug target also has significant implications for the development of new diagnostics for diseases associated with disruptions in protein structure and function. The ability of VPS26C to form a stable complex with DSCR3 and the conservation of the ??-sheet- ??-sheet structure in the protein make it an attractive target for biomarkers that can be used to diagnose diseases associated with these disruptions.

One potential approach to developing a biomarker for VPS26C is the use of techniques such as affinity purification and mass spectrometry to identify proteins that are able to form a stable complex with DSCR3 and have the conserved ??-sheet-??-sheet structure observed in VPS26C. These proteins could then be used as a biomarker for the diagnosis of diseases associated with disruptions in protein structure and function.

Conclusion

In conclusion, the identification of VPS26C as a potential drug target and biomarker for diseases associated with disruptions in protein structure and function has significant implications for the development of new treatments and diagnostics. The unique structure and function of VPS26C, as well as its ability to form a stable complex with DSCR3, make it an attractive target for small molecules and antibodies that can disrupt the protein's stability and function. Further research is needed to develop new treatments and diagnostics based on this discovery.

Protein Name: VPS26 Endosomal Protein Sorting Factor C

Functions: Acts as component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1) (PubMed:28892079). The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes (PubMed:28892079). In the endosomes, drives the retriever and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling (PubMed:28892079)

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•   general information;
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•   the target screening and validation;
•   expression level;
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•   related combination drugs;
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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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