Author: Byeon I-J.L. Yongkiettrakul S. Tsai M-D.
Publisher: Academic Press
ISSN: 0022-2836
Source: Journal of Molecular Biology, Vol.314, Iss.3, 2001-11, pp. : 577-588
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Abstract
It was proposed previously that the FHA2 domain of the yeast protein kinase Rad53 has dual specificity toward pY and pT peptides. The consensus sequences of pY peptides for binding to FHA2, as well as the solution structures of free FHA2 and FHA2 complex with a pY peptide derived from Rad9, have been obtained previously. We now report the use of a pT library to screen for binding of pT peptides with the FHA2 domain. The results show that FHA2 binds favorably to pT peptides with Ile at the +3 position. We then searched the Rad9 sequences with a pTXXI/L motif, and tested the binding affinity of FHA2 toward ten pT peptides derived from Rad9. One of the peptides, 599EVEL(pT)QELP607, displayed the best binding affinity (
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