In silico identification of lipid-binding α helices of uncoupling protein 1

Jing,Ying; Niu,Yahan; Liu,Chang; Zen,Ke; Li,Donghai

doi:10.3892/br.2018.1133

In silico identification of lipid-binding α helices of uncoupling protein 1

Authors:
- Ying Jing
- Yahan Niu
- Chang Liu
- Ke Zen
- Donghai Li
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Affiliations: State Key Laboratory of Pharmaceutical Biotechnology, Jiangsu Engineering Research Center for MicroRNA Biology and Biotechnology, Nanjing Advanced Institute for Life Sciences (NAILS), School of Life Sciences, Nanjing University, Nanjing, Jiangsu 210023, P.R. China
Published online on: July 23, 2018 https://doi.org/10.3892/br.2018.1133
Pages: 313-317
Copyright: © Jing et al. This is an open access article distributed under the terms of Creative Commons Attribution License.

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Abstract

Uncoupling protein 1 (UCP1) located at the mitochondrial inner membrane serves an important role in adaptive non-shivering thermogenesis. Previous data has demonstrated that membrane lipids regulate the biological functions of membrane proteins. However, how mitochondrial lipids interact with UCP1 still remains elusive. In this study, the interactions between UCP1 and membrane lipids were investigated, using bioinformatic approaches due to the limitations associated with experimental techniques. A total of 8 UCP1 peptide regions with α-helices were identified and related to functional sites of UCP1. These were all novel peptide sequences compared with the known protein-lipid interactions. Among several types of UCP1-binding molecules, cardiolipin appeared to serve as a key interacting molecule of the 8 lipid-binding α-helix regions of UCP1. Two cardiolipin-binding lysines (K175 and K269) of UCP1 may be crucial for this UCP1-cardiolipin recognition and UCP1 function. The present findings provide novel insight into the associations of UCP1 with lipids and the potential drug targets in UCP1-associated diseases.

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