1.National Institute of
Biological Sciences, No. 7 Science Park Road, Beijing 102206, China; 2.National Institute of
Biological Sciences, No. 7 Science Park Road, Beijing 102206, China;College of Biological
Sciences and Biotechnology, Tsinghua University, Beijing 100084, China;
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History+
Received
Accepted
Published
2010-07-01
Issue Date
Revised Date
2010-07-01
PDF
(95KB)
Abstract
Recent studies have unequivocally established the link between FTO and obesity. FTO was biochemically shown to belong to the AlkB-like family DNA/RNA demethylase. However, FTO differs from other AlkB members in that it has unique substrate specificity and contains an extended C-terminus with unknown functions. Insight into the substrate selection mechanism and a functional clue to the C-terminus of FTO were gained from recent structural and biochemical studies. These data would be valuable to design FTO-specific inhibitors that can be potentially translated into therapeutic agents for treatment of obesity or obesity-related diseases.
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