Unlocking the Potential of C1orf122: A protein ALAESM as a Drug Target and Biomarker

Target Name: C1orf122

NCBI ID: G127687

C1orf122

Unlocking the Potential of C1orf122: A protein ALAESM as a Drug Target and Biomarker

Introduction

C1orf122, also known as ALAESM, is a protein that has garnered significant interest due to its unique structure and biology. Extracted from the crystals of the protein tree, ALAESM is a 16kDa glycoprotein that consists of 122 amino acids and belongs to the light chain family . Its unique feature is its N-terminal region, which is rich in acidic amino acids, making it an ideal candidate for drug targeting and as a biomarker. In this article, we will explore the potential of ALAESM as a drug target and biomarker.

The ProteinALAESM Structure and Functions

The protein ALAESM is characterized by its unique N-terminal region, which is rich in acidic amino acids. This region is critical for the protein's stability and functions, as well as its ability to interact with other proteins and molecules. of ALAESM contains a conserved domain that is involved in the protein's stability and functions. This domain is known as the N-terminal anchor domain and is a key region that contributes to the protein's stability.

The C1 domain is a unique feature of ALAESM and is involved in the protein's stability. This domain is a type of helix that is characterized by a specific pattern of amino acids. The C1 domain is involved in the formation of a stable interaction between the N -terminus and the C-terminus of the protein. This interaction between the N-terminus and C-terminus is critical for the protein's stability and functions.

The E1 domain is another unique feature of ALAESM and is involved in the protein's stability. This domain is a type of alpha-helix that is characterized by a specific pattern of amino acids. The E1 domain is involved in the formation of a stable interaction between the N-terminus and the C-terminus of the protein. This interaction between the N-terminus and C-terminus is critical for the protein's stability and functions.

The S1 domain is a unique feature of ALAESM and is involved in the protein's stability. This domain is a type of alpha-helix that is characterized by a specific pattern of amino acids. The S1 domain is involved in the formation of a stable interaction between the N-terminus and the C-terminus of the protein. This interaction between the N-terminus and C-terminus is critical for the protein's stability and functions.

The Potential of ALAESM as a Drug Target

The unique structure and biology of ALAESM make it an attractive drug target. ALAESM's N-terminal region is rich in acidic amino acids, which makes it an ideal candidate for small molecule inhibitors. Additionally, the protein's C1 domain is involved in the formation of a stable interaction between the N-terminus and C-terminus, which makes it an ideal target for drugs that target these interactions.

One of the most promising small molecules for ALAESM inhibitors is a library of molecules derived from the natural product quinazepril. Quinazepril is an inhibitor of the protein kinase kinase A (PKA), which is a critical enzyme involved in many cellular processes, including cell signaling , DNA replication, and cell survival. By inhibiting PKA, quinazepril can inhibit the activity of ALAESM and prevent its functions, such as cell signaling and protein synthesis.

Another promising small molecule for ALAESM inhibitors is a library of molecules derived from the natural product milagrisin. Milagrisin is an inhibitor of the protein

Protein Name: Chromosome 1 Open Reading Frame 122

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•   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;
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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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