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5nxq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the carboxy-terminal domain of yeast Ctf4 bound to a stapled Sld5 CIP== | |
| + | <StructureSection load='5nxq' size='340' side='right'caption='[[5nxq]], [[Resolution|resolution]] 2.41Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5nxq]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NXQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.413Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9FZ:(2~{S})-2-azanyl-5-(4-methyl-1,2,3-triazol-1-yl)pentanoic+acid'>9FZ</scene>, <scene name='pdbligand=9G2:(2~{S})-2-azanyl-5-(4-ethyl-1,2,3-triazol-1-yl)pentanoic+acid'>9G2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5nxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nxq OCA], [https://pdbe.org/5nxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nxq RCSB], [https://www.ebi.ac.uk/pdbsum/5nxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nxq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CTF4_YEAST CTF4_YEAST] Accessory factor for DNA replication. It plays a role in accurately duplicating the genome in vivo. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Exploitation of synthetic lethality by small-molecule targeting of pathways that maintain genomic stability is an attractive chemotherapeutic approach. The Ctf4/AND-1 protein hub that links DNA replication, repair and chromosome segregation, represents a novel target for the synthetic lethality approach. Here we report the design, optimization, and validation of double-click stapled peptides encoding the Ctf4-interacting peptide (CIP) of the replicative helicase subunit Sld5. Screening stapling positions in the Sld5 CIP, we identified an unorthodox i,i+6 stapled peptide with improved, sub-micromolar binding to Ctf4. The mode of interaction with Ctf4 was confirmed by a crystal structure of the stapled Sld5 peptide bound to Ctf4. The stapled Sld5 peptide was able to displace the Ctf4-partner DNA polymerase alpha from the replisome in yeast extracts. Our study provides proof-of-principle evidence for the development of small-molecule inhibitors of the human-CTF4 orthologue AND-1. | ||
| - | + | Targeting the genome stability hub Ctf4 by stapled-peptide design.,Wu Y, Villa F, Maman J, Dobnikar L, Lau YH, Simon AC, Labib K, Spring DR, Pellegrini L Angew Chem Int Ed Engl. 2017 Aug 17. doi: 10.1002/anie.201705611. PMID:28815832<ref>PMID:28815832</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5nxq" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Pellegrini L]] | ||
| + | [[Category: Wu Y]] | ||
Current revision
Crystal structure of the carboxy-terminal domain of yeast Ctf4 bound to a stapled Sld5 CIP
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