1qu5
From Proteopedia
(New page: 200px<br /><applet load="1qu5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qu5" /> '''NMR STRUCTURE OF A NEW PHOSPHOTYROSINE BINDI...) |
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| - | [[Image:1qu5.jpg|left|200px]]<br /><applet load="1qu5" size=" | + | [[Image:1qu5.jpg|left|200px]]<br /><applet load="1qu5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qu5" /> | caption="1qu5" /> | ||
'''NMR STRUCTURE OF A NEW PHOSPHOTYROSINE BINDING DOMAIN CONTAINING THE FHA2 DOMAIN OF RAD 53'''<br /> | '''NMR STRUCTURE OF A NEW PHOSPHOTYROSINE BINDING DOMAIN CONTAINING THE FHA2 DOMAIN OF RAD 53'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The forkhead-associated (FHA) domain is a 55-75 amino acid residue module | + | 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== | ==About this Structure== | ||
| - | 1QU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1QU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QU5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Byeon, I | + | [[Category: Byeon, I J.L.]] |
[[Category: Liao, H.]] | [[Category: Liao, H.]] | ||
| - | [[Category: Tsai, M | + | [[Category: Tsai, M D.]] |
[[Category: fha]] | [[Category: fha]] | ||
[[Category: rad53]] | [[Category: rad53]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:45 2008'' |
Revision as of 12:43, 21 February 2008
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NMR STRUCTURE OF A NEW PHOSPHOTYROSINE BINDING DOMAIN CONTAINING THE FHA2 DOMAIN OF RAD 53
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
1QU5 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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