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[[Image:2a0t.gif|left|200px]]
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{{STRUCTURE_2a0t|  PDB=2a0t  |  SCENE=  }}
'''NMR structure of the FHA1 domain of Rad53 in complex with a biological relevant phosphopeptide derived from Madt1'''


==NMR structure of the FHA1 domain of Rad53 in complex with a biological relevant phosphopeptide derived from Madt1==
<StructureSection load='2a0t' size='340' side='right'caption='[[2a0t]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2a0t]] 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=2A0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A0T FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a0t OCA], [https://pdbe.org/2a0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a0t RCSB], [https://www.ebi.ac.uk/pdbsum/2a0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a0t ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a0/2a0t_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2a0t ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Combinatorial library screens based on binding affinity may preferentially select ligands with ability for ionic interactions and miss the biologically relevant ligands that bind more weakly with predominantly hydrophobic interactions.


==Overview==
FHA domain-ligand interactions: importance of integrating chemical and biological approaches.,Mahajan A, Yuan C, Pike BL, Heierhorst J, Chang CF, Tsai MD J Am Chem Soc. 2005 Oct 26;127(42):14572-3. PMID:16231900<ref>PMID:16231900</ref>
Combinatorial library screens based on binding affinity may preferentially select ligands with ability for ionic interactions and miss the biologically relevant ligands that bind more weakly with predominantly hydrophobic interactions.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2A0T is a [[Protein complex]] structure of sequences 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=2A0T OCA].
</div>
<div class="pdbe-citations 2a0t" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
FHA domain-ligand interactions: importance of integrating chemical and biological approaches., Mahajan A, Yuan C, Pike BL, Heierhorst J, Chang CF, Tsai MD, J Am Chem Soc. 2005 Oct 26;127(42):14572-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16231900 16231900]
*[[Protein kinase Spk1|Protein kinase Spk1]]
[[Category: Non-specific serine/threonine protein kinase]]
== References ==
[[Category: Protein complex]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Chang, C F.]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Heierhorst, J.]]
[[Category: Chang C-F]]
[[Category: Mahajan, A.]]
[[Category: Heierhorst J]]
[[Category: Pike, B L.]]
[[Category: Mahajan A]]
[[Category: Tsai, M D.]]
[[Category: Pike BL]]
[[Category: Yuan, C.]]
[[Category: Tsai M-D]]
[[Category: Fha domain. rad53]]
[[Category: Yuan C]]
[[Category: Mdt1]]
[[Category: Nmr]]
[[Category: Phosphoprotein]]
[[Category: Phosphothreonine]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:27:55 2008''