7xzz
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Cryo-EM structure of the nucleosome in complex with p53== | |
+ | <StructureSection load='7xzz' size='340' side='right'caption='[[7xzz]], [[Resolution|resolution]] 4.07Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[7xzz]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XZZ FirstGlance]. <br> | ||
+ | </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=7xzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xzz OCA], [https://pdbe.org/7xzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xzz RCSB], [https://www.ebi.ac.uk/pdbsum/7xzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xzz ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/H31_HUMAN H31_HUMAN] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The tumor suppressor p53 functions as a pioneer transcription factor that binds a nucleosomal target DNA sequence. However, the mechanism by which p53 binds to its target DNA in the nucleosome remains elusive. Here we report the cryo-electron microscopy structures of the p53 DNA-binding domain and the full-length p53 protein complexed with a nucleosome containing the 20 base-pair target DNA sequence of p53 (p53BS). In the p53-nucleosome structures, the p53 DNA-binding domain forms a tetramer and specifically binds to the p53BS DNA, located near the entry/exit region of the nucleosome. The nucleosomal position of the p53BS DNA is within the genomic p21 promoter region. The p53 binding peels the DNA from the histone surface, and drastically changes the DNA path around the p53BS on the nucleosome. The C-terminal domain of p53 also binds to the DNA around the center and linker DNA regions of the nucleosome, as revealed by hydroxyl radical footprinting. These results provide important structural information for understanding the mechanism by which p53 binds the nucleosome and changes the chromatin structure for gene activation. | ||
- | + | Structural basis for p53 binding to its nucleosomal target DNA sequence.,Nishimura M, Takizawa Y, Nozawa K, Kurumizaka H PNAS Nexus. 2022 Sep 4;1(4):pgac177. doi: 10.1093/pnasnexus/pgac177. eCollection , 2022 Sep. PMID:36714865<ref>PMID:36714865</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 7xzz" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Synthetic construct]] | ||
+ | [[Category: Kurumizaka H]] | ||
+ | [[Category: Nishimura M]] | ||
+ | [[Category: Nozawa K]] | ||
+ | [[Category: Takizawa Y]] |
Revision as of 10:36, 15 February 2023
Cryo-EM structure of the nucleosome in complex with p53
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