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Homology Modeling of Perilipin 5
Author(s) -
Niday Zach,
Tansey John
Publication year - 2012
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.26.1_supplement.599.2
Subject(s) - perilipin , homology modeling , lipid droplet , protease , lipase , biochemistry , threading (protein sequence) , protein structure , chemistry , computational biology , biology , enzyme , lipolysis , adipose tissue
The perilipin family of lipid droplet proteins consists of five members. The most recently discovered protein, perilipin 5, also referred to as OXPAT, is primarily found in oxidative tissue and is believed to participate in lipid storage and trafficking within cells. While the protein structures of other proteins in the family, such as TIP47, have been examined, the structure of OXPAT is still unknown; as such, the goal of this project is to obtain data that will help determine its structure. A 200 amino acid segment of the carboxy‐terminus, stretching from residues 206–409, was analyzed using a series of threading programs: SWISS‐MODEL, M4T model, mod web, and I‐TASSER. Predicted structures are indicative of OXPAT 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. Ongoing experiments include crosslinking and protease protection assays, and X‐ray crystallography to confirm the predicted structure. Recent findings indicate that the interaction of OXPAT with the lipase ATGL and its co‐lipase CGI‐58 occurs in the carboxy‐terminus of OXPAT, which substantiates the need for further structural characterization.