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5loi

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5loi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loi OCA], [http://pdbe.org/5loi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5loi RCSB], [http://www.ebi.ac.uk/pdbsum/5loi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5loi ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5loi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loi OCA], [http://pdbe.org/5loi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5loi RCSB], [http://www.ebi.ac.uk/pdbsum/5loi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5loi ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Metabolic products and environmental factors constantly damage DNA. To protect against these insults and maintain genome integrity, cells have evolved mechanisms to repair DNA lesions. One such mechanism involves Rad3, a master kinase coordinating the DNA damage response. Rad26 is a functional subunit of the Rad3-Rad26 complex and responsible for bringing the kinase to sites of DNA damage. Here, I present the crystal structure of Rad26 and identify the elements important for recruiting Rad3. The structure suggests that Rad26 is a dimer with a conserved interface in the N-terminal part of the protein. Biochemical data shows that Rad26 uses its C-terminal domain and the flanking kinase-docking motif to bind specific HEAT repeats in Rad3. Analysis of the reconstituted Rad3-Rad26 heterotetrameric complex with electron microscopy enabled me to propose a structural model for its quaternary structure. In conclusion, these results suggest that Rad26 exists as a dimer and provide crucial insight into how Rad3 is recruited and incorporated into the Rad3-Rad26 DNA repair complex.
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Insights into Rad3 kinase recruitment from the crystal structure of the DNA damage checkpoint protein Rad26.,Andersen KR J Biol Chem. 2017 Mar 17. pii: jbc.M117.780189. doi: 10.1074/jbc.M117.780189. PMID:28314775<ref>PMID:28314775</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 5loi" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 06:47, 5 April 2017

Crystal structure of Myceliophthora thermophila Rad26 (residues 373-841)

5loi, resolution 3.15Å

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