Skip to main content
Fig. 2 | BMC Medical Genomics

Fig. 2

From: A novel likely pathogenic variant in the FBXO32 gene associated with dilated cardiomyopathy according to whole‑exome sequencing

Fig. 2

The image depicts the potential mechanism of FBXO32, as well as the location and conservation of the mutated amino acid. A The different domains of FBXO32 are illustrated here. The image presents a schematic representation of the FBXO32 structure, containing the leucine zipper domain, the leucine-charged residue-rich domain (LCD), nuclear export signal (NES-like motif) in the LCD domain, 2 highly conserved nuclear localization signals (NLS), the F-Box domain (F-Box), the PDZ domain (PDZ), and the Cytochrome c-like domain (CytC). B The mechanism of the importin α3/β-mediated nuclear import of FBXO32 is depicted here. The NLS domain is bound to importin α3; then, importin β binds to importin α3 for transmission through the nuclear pore complex (NPC). C The alignment of conserved NLS residues from different FBXO32 orthologs was compared using the CLUSTALW Web Server. The lysine amino acids are shown in the box

Back to article page

BMC Medical Genomics

ISSN: 1755-8794

Contact us