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1fhr

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(New page: 200px<br /><applet load="1fhr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fhr" /> '''SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD...)
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[[Image:1fhr.gif|left|200px]]<br /><applet load="1fhr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fhr" />
 
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'''SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53 COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE'''<br />
 
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==Overview==
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==SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53 COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE==
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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.
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<StructureSection load='1fhr' size='340' side='right'caption='[[1fhr]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fhr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FHR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhr OCA], [https://pdbe.org/1fhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fhr RCSB], [https://www.ebi.ac.uk/pdbsum/1fhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fhr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RAD53_YEAST RAD53_YEAST] Controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. Phosphorylates proteins on serine, threonine, and tyrosine. Prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. Seems to be involved in the phosphorylation of RPH1.<ref>PMID:8355715</ref> <ref>PMID:7958905</ref> <ref>PMID:10550056</ref> <ref>PMID:11809875</ref> <ref>PMID:15024067</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/1fhr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fhr ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FHR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FHR OCA].
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*[[Protein kinase Spk1|Protein kinase Spk1]]
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== References ==
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==Reference==
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<references/>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10993733 10993733]
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__TOC__
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[[Category: Protein complex]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Byeon, I.J.L.]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Liao, H.]]
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[[Category: Byeon I-JL]]
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[[Category: Tsai, M.D.]]
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[[Category: Liao H]]
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[[Category: Yongkiettrakul, S.]]
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[[Category: Tsai M-D]]
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[[Category: fha domain]]
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[[Category: Yongkiettrakul S]]
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[[Category: phosphoprotein]]
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[[Category: phosphotyrosine]]
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[[Category: rad53]]
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[[Category: rad9]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:55:57 2007''
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Current revision

SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53 COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE

PDB ID 1fhr

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