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Sci. Signal., 23 December 2008
Vol. 1, Issue 51, p. re12
[DOI: 10.1126/scisignal.151re12]

REVIEWS

Structure and Function of the Phosphothreonine-Specific FHA Domain

Anjali Mahajan1, Chunhua Yuan2, Hyun Lee1,3, Eric S.-W. Chen3,4,5, Pei-Yu Wu5, and Ming-Daw Tsai1,2,3,4,5*

1 Biophysics Program, Ohio State University, Columbus, OH 43210, USA.
2 Campus Chemical Instrument Center, Ohio State University, Columbus, OH 43210, USA.
3 Genomics Research Center, Academia Sinica, Taipei 115, Taiwan.
4 Institute of Biochemical Science, National Taiwan University, Taipei 10617, Taiwan.
5 Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan.

Gloss: The forkhead-associated (FHA) domain is a signaling domain present in various proteins from prokaryotes and eukaryotes. It interacts with other proteins on the basis of its ability to specifically recognize phosphothreonine residues. Proteins that contain the FHA domain play important functional roles in such processes as protein kinase signaling, cell cycle regulation, and DNA damage response. It is now evident that interference with the binding capabilities of these domains can elicit abnormal cellular responses. Detailed structural analyses have led to an understanding of the structural bases of the biological functions of the FHA domain. Information about this structure-function relationship will be useful in understanding the signaling mechanisms that involve FHA domains and, potentially, in the design of therapeutics.

* Corresponding author. E-mail: mdtsai{at}gate.sinica.edu.tw

Citation: A. Mahajan, C. Yuan, H. Lee, E. S.-W. Chen, P.-Y. Wu, M.-D. Tsai, Structure and Function of the Phosphothreonine-Specific FHA Domain. Sci. Signal. 1, re12 (2008).


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