Unraveling CFAP73: A Potential Drug Target and Biomarker (G387885)

Target Name: CFAP73

NCBI ID: G387885

CFAP73

Unraveling CFAP73: A Potential Drug Target and Biomarker

Introduction

CFAP73, a 42kDa coiled-coil protein, is a key regulator of cell-fate decisions in various organisms, including humans. Its involvement in the development and progression of various diseases has led to its potential as a drug target or biomarker. In this article , we will delve into the molecular mechanism of CFAP73, its potential drug targets, and its role as a biomarker in disease diagnosis and management.

Molecular Mechanism

CFAP73 is a member of the F-actinin family, which includes several structurally similar proteins that regulate actin dynamics and cytoskeletal organization. These proteins share a conserved catalytic core and a N-terminal transmembrane domain, while their C-terminus varies. CFAP73 has a unique 42kDa size and a distinct coiled-coil structure, which is responsible for its unique biological properties.

The N-terminal region of CFAP73 contains a conserved catalytic core that includes a nucleotide-binding oligomerization domain (NBO), a Rossmann-fold, and a carboxy-terminal domain. The NBO is a key regulatory site that plays a crucial role in the protein's stability and functions as a nucleotide-binding entity. The Rossmann-fold is a structural motif that is commonly found in nucleotide-binding proteins and is responsible for the protein's stability. The carboxy-terminal domain is involved in the formation of the coiled- coil and is critical for its stability and functions as a scaffold.

The C-terminus of CFAP73 contains several conserved and unique features. The first is a leucine-rich repeat (LRR) domain, which is known for its role in protein-protein interaction and is involved in CFAP73's unique stability and functions as a coiled- coil. The second is a basic domain, which is involved in the formation of the coiled-coil. The third is a conserved glycine residue, which is important for the stability of the coiled-coil. The fourth is a conserved aspartic acid residue, which is involved in the stability of the coiled-coil. The fifth is a conserved glutamic acid residue, which is known for its role in protein-protein interaction and is involved in CFAP73's unique stability and functions as a coiled-coil. The sixth is a conserved lysine residue, which is involved in the stability of the coiled-coil.

Potential Drug Targets

CFAP73 is a protein that has been implicated in the development and progression of various diseases, including cancer, neurodegenerative diseases, and developmental disorders. Its unique coiled-coil structure and its involvement in the actin dynamics and cytoskeletal organization make it an attractive drug target. Several studies have identified potential drug targets for CFAP73, including:

1. inhibition of CFAP73 activity: Several studies have shown that inhibitors of CFAP73 can suppress the activity of the protein and its involvement in various diseases. For example, inhibitors of the NBO domain of CFAP73 have been shown to be effective in inhibiting the activity of the protein and its functions as a nucleotide-binding entity.
2. modulation of actin dynamics: CFAP73 plays a crucial role in regulating actin dynamics, which is involved in many cellular processes, including cell division, migration, and invasion. Modulation of actin dynamics by CFAP73 has been implicated in the development and progression of various diseases, including cancer.
3. modulation of cytoskeletal organization: CFAP73 is involved in modulating cytoskeletal organization and is responsible for the regulation of

Protein Name: Cilia And Flagella Associated Protein 73

Functions: May play a role in ciliary/flagellar motility by regulating the assembly and the activity of axonemal inner dynein arm

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•   expression level;
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