Emopamil binding protein

Ideogram human chromosome X

Emopamil binding protein

Emopamil binding protein (EBP) is a protein that in humans is encoded by the EBP gene. EBP is an integral membrane protein that is localized in the endoplasmic reticulum. It plays a crucial role in the biosynthesis of cholesterol by catalyzing the conversion of delta-8,14-sterol to lathosterol in the Bloch pathway.

Structure

EBP is composed of 25 exons and spans approximately 50 kb of genomic DNA. The protein consists of 429 amino acids and contains multiple transmembrane domains that anchor it to the endoplasmic reticulum membrane.

Function

The primary function of EBP is to catalyze the conversion of delta-8,14-sterol to lathosterol, a key step in the cholesterol biosynthesis pathway. This enzymatic activity is essential for the production of cholesterol, which is a critical component of cell membranes and a precursor for the synthesis of steroid hormones.

Clinical significance

Mutations in the EBP gene can lead to a rare genetic disorder known as chondrodysplasia punctata 2 (CDPX2). Individuals with CDPX2 exhibit skeletal abnormalities, growth retardation, and characteristic skin changes due to impaired cholesterol biosynthesis. Understanding the role of EBP in cholesterol metabolism is crucial for the development of potential therapeutic interventions for CDPX2.

Interactions

EBP has been shown to interact with several other proteins involved in cholesterol biosynthesis, such as 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) and sterol regulatory element-binding proteins (SREBPs). These interactions are essential for coordinating the various steps of cholesterol synthesis and maintaining cellular lipid homeostasis.