Overview of MRFAP1: Structure, Function and Potential as A Drug Target

Target Name: MRFAP1

NCBI ID: G93621

Overview of MRFAP1: Structure, Function and Potential as A Drug Target

Mutations in the gene PAM14 (Protein-Protein Interaction gene 14) have been linked to a range of human diseases, including neurodegenerative disorders, autoimmune diseases, and psychiatric conditions. The protein encoded by PAM14, known as MRFAP1 (MutL homolog 1), plays a crucial role in cellular signaling and has been implicated in numerous cellular processes, including neuronal communication, inflammation, and stress response.

Despite the growing body of research on MRFAP1 and its potential role in disease, much of our understanding of this protein remains unraveled. The functional consequences of PAM14 mutations have not been fully understood, and the development of new therapeutic approaches for these mutations remains a major focus of research.

In this article, we will provide an overview of MRFAP1, including its structure, function, and potential as a drug target. We will discuss the current state of research on MRFAP1 mutations and the challenges and opportunities for the future of this field.

Structure and Function

MRFAP1 is a protein that belongs to the family of protein-protein interaction (PPI) proteins. PPI proteins are involved in the regulation of protein-protein interactions and play a crucial role in cellular signaling. They are composed of multiple domains, including an extracellular domain, a transmembrane domain, and an intracellular domain.

The extracellular domain of MRFAP1 consists of a long N-terminal region that contains a leucine-rich repeat (LRR) and a putative G-protein-coupled receptor (GPCR) domain. The LRR and GPCR domains are involved in the formation of inclusion loops , which are conserved in many PPI proteins and play a role in increasing the stability and stability of the protein.

The transmembrane domain of MRFAP1 contains a transmembrane protein (TMP) domain and a unique N-terminal region that is involved in the formation of a disulfide bond. The TMP domain is involved in the regulation of the cytoskeleton and is conserved in many PPI proteins. The N-terminal region is involved in the regulation of protein-protein interactions and is known as the PAM14-related domain (PR domain).

The intracellular domain of MRFAP1 contains a nucleotide-binding oligomerization (NBO) domain, which is involved in the regulation of DNA binding and is conserved in many proteins. The NBO domain is also involved in the regulation of protein-protein interactions and is known as the PAM14-related domain (PR domain).

PAM14 Mutations and their Implications

Several mutations have been identified in the PAM14 gene, including missense (Ala-substitution), nonsense (Glu-substitution), and splice variants. These mutations have been implicated in a range of human diseases, including neurodegenerative disorders, autoimmune diseases, and psychiatric conditions.

The missense mutation, which results in the substitution of the amino acid Asp for Asn at position 692, has been linked to a range of neurodegenerative disorders, including Alzheimer's disease, Parkinson's disease, and Huntington's disease. The Asp-to-Asn substitution is known to alter the stability and localization of the PAM14 protein and may contribute to the misfolding and subsequent degradation of the protein.

The nonsense mutation, which results in the substitution of the amino acid Asp for Asn at position 216, has been implicated in a range of autoimmune diseases, including type 1 diabetes, multiple sclerosis, and rheumatoid arthritis. The Asp-to-Asn substitution is Known to alter the structure and function of the PAM14 protein and may contribute to the development of autoimmune diseases.

The splice variant is a type of mutation that results in the substitution of one or more exons in the

Protein Name: Morf4 Family Associated Protein 1

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