Structural basis for the binding of DNP and purine nucleotides onto UCP1

Uncoupling protein 1 (UCP1) conducts protons through the inner mitochondrial membrane to uncouple mitochondrial respiration from ATP production, thereby converting the electrochemical gradient of protons into heat 1 , 2 . The activity of UCP1 is activated by endogenous fatty acids and synthetic smal...

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Bibliographic Details
Published in:	Nature (London) Vol. 620; no. 7972; pp. 226 - 231
Main Authors:	Kang, Yunlu, Chen, Lei
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 03.08.2023 Nature Publishing Group
Subjects:	101/28 2,4-Dinitrophenol 2,4-Dinitrophenol - chemistry 2,4-Dinitrophenol - metabolism 631/45/612/1237 631/535/1258/1259 82/80 82/83 Adenosine triphosphate Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism ATP Binding sites Cell Membrane - metabolism Cytosol - metabolism Electrochemistry Electron transport Fatty acids Fatty Acids - metabolism Humanities and Social Sciences Humans Lipids multidisciplinary Nucleotides Permeability Protein Conformation Proteins Protons Respiration Science Science (multidisciplinary) Uncoupling protein 1 Uncoupling Protein 1 - chemistry Uncoupling Protein 1 - metabolism
ISSN:	0028-0836, 1476-4687, 1476-4687
Online Access:	Get full text
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