Good news! It took only 40 years of research (caution: irony)! I have a hunch that this is still early stage research (see also the abstract).
But what about white fat, the article is totally mum about it?
"A new study ... is the first to reveal the molecular structure of a protein called ‘Uncoupling protein 1’ (UCP1).
This protein allows brown fat tissue, or ‘good fat’, to burn off calories as heat – in contrast to conventional white fat that stores calories. ...
The team say that their findings provide crucial molecular details that will help develop therapeutics that activate UCP1 artificially to burn off excess calories from fat and sugar. ...
“Our paper reveals, for the first time, the structure of UCP1 in atomic detail, and how its activity in brown fat cells is inhibited by a key regulatory molecule.” ...
“This is an exciting development that follows more than four decades of research into what UCP1 looks like and how it works,” ...
A lot of research has been focusing on finding ways to encourage brown fat and how to turn white fat into brown fat – in order to burn more calories and fight metabolic disease. ..."
“Our paper reveals, for the first time, the structure of UCP1 in atomic detail, and how its activity in brown fat cells is inhibited by a key regulatory molecule.” ...
“This is an exciting development that follows more than four decades of research into what UCP1 looks like and how it works,” ...
A lot of research has been focusing on finding ways to encourage brown fat and how to turn white fat into brown fat – in order to burn more calories and fight metabolic disease. ..."
From the abstract:
"Mitochondrial uncoupling protein 1 (UCP1) gives brown adipose tissue of mammals its specialized ability to burn calories as heat for thermoregulation. When activated by fatty acids, UCP1 catalyzes the leak of protons across the mitochondrial inner membrane, short-circuiting the mitochondrion to generate heat, bypassing ATP synthesis. In contrast, purine nucleotides bind and inhibit UCP1, regulating proton leak by a molecular mechanism that is unclear. We present the cryo–electron microscopy structure of the GTP-inhibited state of UCP1, which is consistent with its nonconducting state. The purine nucleotide cross-links the transmembrane helices of UCP1 with an extensive interaction network. Our results provide a structural basis for understanding the specificity and pH dependency of the regulatory mechanism. UCP1 has retained all of the key functional and structural features required for a mitochondrial carrier–like transport mechanism. The analysis shows that inhibitor binding prevents the conformational changes that UCP1 uses to facilitate proton leak."
Fig. 1. Functional and structural properties of human UCP1.
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