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Homology modeling of perilipin 5 (606.8)
Author(s) -
Sarr Aboubackrine,
Bennett Jennifer,
Niday Zach,
Tansey John
Publication year - 2014
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.28.1_supplement.606.8
Subject(s) - perilipin , lipid droplet , hormone sensitive lipase , biochemistry , chemistry , phosphorylation , homology modeling , amphiphysin , microbiology and biotechnology , lipase , biology , enzyme , cell , lipolysis , adipose tissue , endocytosis , dynamin
Lipid storage droplets (LSD) regulate the storage of triacylglycerols and cholesteryl esters in the eukaryotic cell. The Perilipin family is a group of five conserved genes coding for LSD‐binding proteins. At least one perilipin has been found in the coat of all currently known LSD. The goal of the project is to generate a threaded model of perilipin 5 from existing structures in the Protein Data Bank, identify putative conserved domains or folds in perilipin 5, and identify the location of important residues (such as phosphorylation sites) in the proposed model . The amino acid sequence of perilipin 5 was entered into threading programs RaptorX and itasser in attempt to find conserved domains. Predicted structures are indicative of perilipin 5 being approximately 80% α‐helical for the analyzed segment. Associated QMEAN4 scores ranged from 0.50‐0.83, indicating the homological models are reliable predictions. The interaction of perilipin 5 with the lipase ATGL and its co‐lipase CGI‐58 occurs in the carboxy‐terminus, which substantiates the need for further structural characterization of this domain.