1dmz
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(New page: 200px<br /><applet load="1dmz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dmz" /> '''A REFINED NMR STRUCTURE OF A NEW PHOPHOPEPTI...)
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Revision as of 11:18, 20 November 2007
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A REFINED NMR STRUCTURE OF A NEW PHOPHOPEPTIDE-BINDING DOMAIN CONTAINING THE FHA2 OF RAD53
Overview
The forkhead-associated (FHA) domain is a 55-75 amino acid residue module, found in >20 proteins from yeast to human. It has been suggested to, participate in signal transduction pathways, perhaps via protein-protein, interactions involving recognition of phosphopeptides. Neither the, structure nor the ligand of FHA is known. Yeast Rad53, a checkpoint, protein involved in DNA damage response, contains two FHA domains, FHA1, (residues 66-116) and FHA2 (residues 601-664), the second of which, recognizes phosphorylated Rad9. We herein report the solution structure of, an "FHA2-containing domain" of Rad53 (residues 573-730). The structure, consists of a beta-sandwich containing two antiparallel beta-sheets and a, short, C-terminal alpha-helix. Binding experiments suggested that the, FHA2-containing domain specifically recognizes pTyr and a pTyr-containing, peptide from Rad9, and that the binding site involves residues highly, conserved across FHA domains. The results, along with other recent, reports, suggest that FHA domains could have pTyr and pSer/Thr dual, specificity.
About this Structure
1DMZ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53., Liao H, Byeon IJ, Tsai MD, J Mol Biol. 1999 Dec 10;294(4):1041-9. PMID:10588905
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