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Elucidation of the N‐terminal Structure and Characteristics of Perilipin 5
Author(s) -
Wei Derek T.,
Tansey John T.
Publication year - 2018
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.2018.32.1_supplement.814.9
Subject(s) - perilipin , lipid droplet , biology , biochemistry , chemistry , adipose tissue , lipolysis
The United States and other nations are experiencing an epidemic of lipid‐related diseases. Understanding the etiologies of these diseases is an increasingly imperative objective. Finding the function and mechanisms of the molecules involved in these lipid‐related diseases could show new and enhanced treatments for those suffering from these conditions. The perilipins, a family of five conserved lipid droplet proteins, are a chief subject of study in this field. However, an abundance of structural data is absent and would facilitate major strides in clarifying perilipin function. There is three‐dimensional structural data on the carboxyl terminus of one member in the perilipin family, perilipin 3, but not for other family members. The current study is aimed to characterize and determine the structure of the N‐terminal domain of perilipin 5. Perilipin 5 is of interest because of its implications in numerous of the metabolic conditions observed in the population. The N‐terminus is the concentration of the project because the C‐terminus of the protein has a high sequence homology with that of perilipin 3. Therefore, the C‐terminus of perilipin 5 is predicted to take on a similar structure to the C‐terminus of perilipin 3. A cDNA fragment coding for the N‐terminal region of perilipin 5 was PCR amplified from the full‐length Mus musculus perilipin 5 gene. It was then transformed into Escherichia Coli to produce the protein fragment of interest. Isolation of the protein fragment is undergoing via nickel affinity chromatography. Theoretical secondary and tertiary structures of the N‐terminal fragment of perilipin 5 have been obtained using the programs Phyre2, SCRATCH, GOR4, CFSSP, and Jpred. Computer models predict the sequence's secondary structure to contain numerous alpha helices with increasing frequency near the back half of the fragment. In conclusion, determination of the N‐terminal structure of perilipin 5 will further enable research into the functions of the perilipin family. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .