6hm4: Difference between revisions
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==Crystal structure of Rad4 BRCT1,2 in complex with a Mdb1 phosphopeptide== | ==Crystal structure of Rad4 BRCT1,2 in complex with a Mdb1 phosphopeptide== | ||
<StructureSection load='6hm4' size='340' side='right' caption='[[6hm4]], [[Resolution|resolution]] 1.77Å' scene=''> | <StructureSection load='6hm4' size='340' side='right'caption='[[6hm4]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6hm4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HM4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6hm4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HM4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.770186Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6hm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hm4 OCA], [https://pdbe.org/6hm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hm4 RCSB], [https://www.ebi.ac.uk/pdbsum/6hm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hm4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RAD4_SCHPO RAD4_SCHPO] Essential component for DNA replication and also the checkpoint control system which couples S and M phases. May directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6hm4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6hm4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[DNA repair protein Rad4|DNA repair protein Rad4]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Schizosaccharomyces pombe 972h-]] | ||
[[Category: | [[Category: Day M]] | ||
[[Category: | [[Category: Oliver AW]] | ||
[[Category: | [[Category: Pearl LH]] | ||
[[Category: | [[Category: Rappas M]] | ||
Latest revision as of 08:18, 21 November 2024
Crystal structure of Rad4 BRCT1,2 in complex with a Mdb1 phosphopeptideCrystal structure of Rad4 BRCT1,2 in complex with a Mdb1 phosphopeptide
Structural highlights
FunctionRAD4_SCHPO Essential component for DNA replication and also the checkpoint control system which couples S and M phases. May directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Publication Abstract from PubMedTOPBP1 and its fission yeast homologueRad4, are critical players in a range of DNA replication, repair and damage signalling processes. They are composed of multiple BRCT domains, some of which bind phosphorylated motifs in other proteins. They thus act as multi-point adaptors bringing proteins together into functional combinations, dependent on post-translational modifications downstream of cell cycle and DNA damage signals. We have now structurally and/or biochemically characterised a sufficient number of high-affinity complexes for the conserved N-terminal region of TOPBP1 and Rad4 with diverse phospho-ligands, including human RAD9 and Treslin, and Schizosaccharomyces pombe Crb2 and Sld3, to define the determinants of BRCT domain specificity. We use this to identify and characterise previously unknown phosphorylation-dependent TOPBP1/Rad4-binding motifs in human RHNO1 and the fission yeast homologue of MDC1, Mdb1. These results provide important insights into how multiple BRCT domains within TOPBP1/Rad4 achieve selective and combinatorial binding of their multiple partner proteins. BRCT domains of the DNA damage checkpoint proteins TOPBP1/Rad4 display distinct specificities for phosphopeptide ligands.,Day M, Rappas M, Ptasinska K, Boos D, Oliver AW, Pearl LH Elife. 2018 Oct 8;7. pii: 39979. doi: 10.7554/eLife.39979. PMID:30295604[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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