1g3g
From Proteopedia
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NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53
Overview
Forkhead-associated (FHA) domains have been shown to recognize both pThr, and pTyr-peptides. The solution structures of the FHA2 domain of Rad53, from Saccharomyces cerevisiae, and its complex with a pTyr peptide, have, been reported recently. We now report the solution structure of the other, FHA domain of Rad53, FHA1 (residues 14-164), and identification of binding, sites of FHA1 and its target protein Rad9. The FHA1 structure consists of, 11 beta-strands, which form two large twisted anti-parallel beta-sheets, folding into a beta-sandwich. Three short alpha-helices were also, identified. The beta-strands are linked by several loops and turns. These, structural features of free FHA1 are similar to those of free FHA2, but, there are significant differences in the loops. Screening of a peptide, library [XXX(pT)XXX] against FHA1 revealed an absolute requirement for Asp, at the +3 position and a preference for Ala at the +2 position. These two, criteria are met by a pThr motif (192)TEAD(195) in Rad9. Surface plasmon, resonance analysis showed that a pThr peptide containing this motif, (188)SLEV(pT)EADATFVQ(200) from Rad9, binds to FHA1 with a K(d) value of, 0.36 microM. Other peptides containing pTXXD sequences also bound to FHA1, but less tightly (K(d)=4-70 microM). These results suggest that Thr192 of, Rad9 is the likely phosphorylation site recognized by the FHA1 domain of, Rad53. The tight-binding peptide was then used to identify residues of, FHA1 involved in the interaction with the pThr peptide. The results are, compared with the interactions between the FHA2 domain and a pTyr peptide, derived from Rad9 reported previously.
About this Structure
1G3G is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of the FHA1 domain of yeast Rad53 and identification of binding sites for both FHA1 and its target protein Rad9., Liao H, Yuan C, Su MI, Yongkiettrakul S, Qin D, Li H, Byeon IJ, Pei D, Tsai MD, J Mol Biol. 2000 Dec 15;304(5):941-51. PMID:11124038
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