1m18

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{{STRUCTURE_1m18| PDB=1m18 | SCENE= }}
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==LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA==
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===LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA===
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<StructureSection load='1m18' size='340' side='right' caption='[[1m18]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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{{ABSTRACT_PUBMED_12559907}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1m18]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M18 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1SZ:N-[5-[[4-[[5-[[5-[[5-[[5-[[3-[3-(DIMETHYLAMINO)PROPYLAMINO]-3-OXIDANYLIDENE-PROPYL]CARBAMOYL]-1-METHYL-PYRROL-3-YL]CARBAMOYL]-1-METHYL-PYRROL-3-YL]CARBAMOYL]-1-METHYL-PYRROL-3-YL]CARBAMOYL]-1-METHYL-PYRROL-3-YL]AMINO]-4-OXIDANYLIDENE-BUTYL]CARBAMOYL]-1-METHYL-PYRROL-3-YL]-1-METHYL-4-[[1-METHYL-4-[(1-METHYLIMIDAZOL-2-YL)CARBONYLAMINO]PYRROL-2-YL]CARBONYLAMINO]IMIDAZOLE-2-CARBOXAMIDE'>1SZ</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aoi|1aoi]], [[1m19|1m19]], [[1m1a|1m1a]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m18 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m18 RCSB], [http://www.ebi.ac.uk/pdbsum/1m18 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m18_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We determined the crystal structures of three nucleosome core particles in complex with site-specific DNA-binding ligands, the pyrrole-imidazole polyamides. While the structure of the histone octamer and its interaction with the DNA remain unaffected by ligand binding, nucleosomal DNA undergoes significant structural changes at the ligand-binding sites and in adjacent regions to accommodate the ligands. Our findings suggest that twist diffusion occurs over long distances through tightly bound nucleosomal DNA. This may be relevant to the mechanism of ATP-dependent and spontaneous nucleosome translocation, and to the effect of bound factors on nucleosome dynamics.
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==Function==
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Crystal structures of nucleosome core particles in complex with minor groove DNA-binding ligands.,Suto RK, Edayathumangalam RS, White CL, Melander C, Gottesfeld JM, Dervan PB, Luger K J Mol Biol. 2003 Feb 14;326(2):371-80. PMID:12559907<ref>PMID:12559907</ref>
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[[http://www.uniprot.org/uniprot/H2A1_XENLA H2A1_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H32_XENLA H32_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H2B11_XENLA H2B11_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[1m18]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M18 OCA].
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</div>
==See Also==
==See Also==
*[[Histone|Histone]]
*[[Histone|Histone]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:012559907</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Dervan, P B.]]
[[Category: Dervan, P B.]]

Revision as of 04:23, 3 October 2014

LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA

1m18, resolution 2.45Å

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