1fhq

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[[Image:1fhq.gif|left|200px]]
 
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{{Structure
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==REFINED SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53==
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|PDB= 1fhq |SIZE=350|CAPTION= <scene name='initialview01'>1fhq</scene>
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<StructureSection load='1fhq' size='340' side='right'caption='[[1fhq]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1fhq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FHQ FirstGlance]. <br>
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|ACTIVITY=
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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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|GENE=
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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=1fhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhq OCA], [https://pdbe.org/1fhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fhq RCSB], [https://www.ebi.ac.uk/pdbsum/1fhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fhq ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1fhr|1FHR]], [[1dmz|1DMZ]], [[1qu5|1QU5]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhq OCA], [http://www.ebi.ac.uk/pdbsum/1fhq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fhq RCSB]</span>
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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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}}
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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/1fhq_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=1fhq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''REFINED SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53'''
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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:10993733<ref>PMID:10993733</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1fhq" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Protein kinase Spk1|Protein kinase Spk1]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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://www.ncbi.nlm.nih.gov/pubmed/10993733 10993733]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Byeon I-JL]]
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[[Category: Byeon, I J.L.]]
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[[Category: Liao H]]
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[[Category: Liao, H.]]
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[[Category: Tsai M-D]]
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[[Category: Tsai, M D.]]
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[[Category: fha domain]]
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[[Category: phosphoprotein]]
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[[Category: phosphotyrosine]]
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[[Category: rad53]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:23:05 2008''
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Current revision

REFINED SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53

PDB ID 1fhq

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