Fig. 1: Gene structure, protein domains, and 3D structure of human CYP51A1. | Cell Death Discovery

Fig. 1: Gene structure, protein domains, and 3D structure of human CYP51A1.

From: CYP51A1 in health and disease: from sterol metabolism to regulated cell death

Fig. 1

A Schematic representation of the CYP51A1 gene structure, showing the promoter region, exons (green), and introns (purple). The gene consists of 10 exons, with Exon 1 and Exon 10 contributing to the 5′ and 3′ untranslated regions (UTRs), respectively. B Domain architecture of the CYP51A1 protein, highlighting the signal peptide (residues 1–21) and the transmembrane region (residues 28–50) at the N-terminus. The conserved cytochrome P450 domain (Pfam 67–502) is shaded in gray. Positions of intron–exon boundaries and their associated splicing phases are indicated along the linear protein structure. C Ribbon diagram of the CYP51A1 3D structure (PDB ID: 4UHL), showing the binding of the ligand to the α-helix structure. This structure provides insights into the active site and potential ligand-binding regions critical for its sterol 14α-demethylase activity.

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