Comparative study of Dog and Human Lipid Droplet-associated protein (PLIN2)

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Abstract

Intracellular lipid droplets (LDs) are vital organelles that store energy, manage oxidative stress, and coordinate cellular signaling. A key protein family associated with LDs is the perilipins, with perilipin 2 (PLIN2) being prominent. This study focuses on a comparative analysis of canine and human PLIN2 to understand their structural and functional similarities. The genomic data for PLIN2 in both species were curated, revealing location, transcripts, exons, and introns. Sequence analysis demonstrated 85% identity between dog and human PLIN2, with conserved residues essential for structural and functional roles. Amino acid composition analysis revealed similarities in charged residues and in stabilizing and destabilizing residues. Despite their structural similarities (72% common secondary structure elements), a 3D comparison revealed significant differences in conformation. Physicochemical properties, including stability indices, were found to be distinct, possibly influencing their interactions. The study highlights the conservation of PLIN2’s functional regions, shedding light on its role in protecting LDs from degradation across species.

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