1fhq
From Proteopedia
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| - | [[Image:1fhq.gif|left|200px]] | + | [[Image:1fhq.gif|left|200px]] |
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| - | '''REFINED SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53''' | + | {{Structure |
| + | |PDB= 1fhq |SIZE=350|CAPTION= <scene name='initialview01'>1fhq</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''REFINED SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FHQ is a [ | + | 1FHQ is a [[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=1FHQ OCA]. |
==Reference== | ==Reference== | ||
| - | II. Structure and specificity of the interaction between the FHA2 domain of Rad53 and phosphotyrosyl peptides., Wang P, Byeon IJ, Liao H, Beebe KD, Yongkiettrakul S, Pei D, Tsai MD, J Mol Biol. 2000 Sep 29;302(4):927-40. PMID:[http:// | + | II. Structure and specificity of the interaction between the FHA2 domain of Rad53 and phosphotyrosyl peptides., Wang P, Byeon IJ, Liao H, Beebe KD, Yongkiettrakul S, Pei D, Tsai MD, J Mol Biol. 2000 Sep 29;302(4):927-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10993733 10993733] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rad53]] | [[Category: rad53]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:09:13 2008'' |
Revision as of 09:09, 20 March 2008
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REFINED SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53
Overview
The forkhead-associated (FHA) domain is a protein module found in many proteins involved in cell signaling in response to DNA damage. It has been suggested to bind to pThr sites of its target protein. Recently we have determined the first structure of an FHA domain, FHA2 from the yeast protein Rad53, and demonstrated that FHA2 binds to a pTyr-containing peptide (826)EDI(pY)YLD(832) from Rad9, with a moderate affinity (K(d) ca. 100 microM). We now report the solution structure of the complex of FHA2 bound with this pTyr peptide. The structure shows that the phosphate group of pTyr interacts directly with three arginine residues (605, 617, and 620), and that the leucine residue at the +2 position from the pTyr interacts with a hydrophobic surface on FHA2. The sequence specificity of FHA2 was determined by screening a combinatorial pTyr library. The results clearly show that FHA2 recognizes specific sequences C-terminal to pTyr with the following consensus: XX(pY)N(1)N(2)N(3), where N(1)=Leu, Met, Phe, or Ile, N(2)=Tyr, Phe, Leu, or Met, and N(3)=Phe, Leu, or Met. Two of the selected peptides, GF(pY)LYFIR and DV(pY)FYMIR, bind FHA2 with K(d) values of 1.1 and 5.0 microM, respectively. The results, along with other recent reports, demonstrate that the FHA domain is a new class of phosphoprotein-binding domain, capable of binding both pTyr and pThr sequences.
About this Structure
1FHQ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
II. Structure and specificity of the interaction between the FHA2 domain of Rad53 and phosphotyrosyl peptides., Wang P, Byeon IJ, Liao H, Beebe KD, Yongkiettrakul S, Pei D, Tsai MD, J Mol Biol. 2000 Sep 29;302(4):927-40. PMID:10993733
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