A loop matters for FTO substrate selection.
10.1007/s13238-010-0082-2
- Author:
Zhifu HAN
1
;
Ning HUANG
;
Tianhui NIU
;
Jijie CHAI
Author Information
1. National Institute of Biological Sciences, No. 7 Science Park Road, Beijing, 102206, China.
- Publication Type:Journal Article
- MeSH:
AlkB Homolog 1, Histone H2a Dioxygenase;
Alpha-Ketoglutarate-Dependent Dioxygenase FTO;
Amino Acid Motifs;
Animals;
Catalytic Domain;
DNA;
metabolism;
DNA Repair Enzymes;
metabolism;
Humans;
Methylation;
Obesity;
genetics;
Proteins;
chemical synthesis;
classification;
genetics;
RNA;
metabolism;
Substrate Specificity
- From:
Protein & Cell
2010;1(7):616-620
- CountryChina
- Language:English
-
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.
