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Characterization of the Perilipin 5 C‐Terminus
Author(s) -
Clinton Tim D,
Wei Derek T,
Tansey John T
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.490.2
Subject(s) - perilipin , lipid droplet , chemistry , medicine , adipose tissue , lipolysis
Many countries around the globe have been plagued with a recent epidemic in lipid‐associated diseases. These diseases include obesity, diabetes, and non‐alcoholic fatty liver disease among many others. The United States itself has fallen heavily victim to these ailments, placing first in worldwide rankings for obese persons and within the top fiftieth in rankings for the percentage of persons afflicted with diabetes. These diseases pose clear threats to modern society and having a greater understanding of the mechanistic background of them may lead to better treatments options for those afflicted. A common thread through all these devastating illnesses is their connection to lipids and more specifically lipid storage. Cellular lipids are stored in lipid storage droplets, and these droplets are coated by the perilipins, five regulatory proteins that have an integral role in regulating the breakdown of fats. One such of these family members is perilipin 3, a protein that's structure has been partially determined. In Perilipin 5 this structure has not been determined and is the current focus of this study. Previously a crystal structure of the C‐terminal region of perilipin 3 was determined for residues 206 to 431. These regions were aligned with perilipin 5 using BLAST and their analogous location within the Perilipin 5 DNA sequence was determined. This region of perilipin 5 is being expressed as a 6‐his fusion protein for subsequent characterization and structure determination. Using the predicative programs RaptorX and Phyre2 theoretical protein structures were compiled. These were labeled for regions of interest including a putative hydrophobic cleft found in perilipin 3 that was previously found to recruit that protein to lipid droplets. Collectively these findings indicate that it is highly likely that perilipin 5 has a similar structure to perilipin 3 in the carboxy terminus. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .