Protein & Cell >

2010 , Vol. 1 >Issue 7: 616 - 620

DOI: https://doi.org/10.1007/s13238-010-0082-2

Research articles

A loop matters for FTO substrate selection

Expand
  • 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;

Published date: 01 Jul 2010

Fold

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.

Cite this article

Zhifu Han, Ning Huang, Tianhui Niu, Jijie Chai, . A loop matters for FTO substrate selection[J]. Protein & Cell, 2010 , 1(7) : 616 -620 . DOI: 10.1007/s13238-010-0082-2

Options
Outlines

/

〈 〉