382d

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[[Image:382d.png|left|200px]]
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==HYDRATION AND RECOGNITION OF METHYLATED CPG STEPS IN DNA.==
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<StructureSection load='382d' size='340' side='right' caption='[[382d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[382d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=382D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=382D FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
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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=382d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=382d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=382d RCSB], [http://www.ebi.ac.uk/pdbsum/382d PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The analysis of the hydration pattern around methylated CpG steps in three high resolution (1.7, 2.15 and 2.2 A) crystal structures of A-DNA decamers reveals that the methyl groups of cytosine residues are well hydrated. In comparing the native structure with two structurally distinct forms of the decamer d(CCGCCGGCGG) fully methylated at its CpG steps, this study shows also that in certain structural and sequence contexts, the methylated cytosine base can be more hydrated that the unmodified one. These water molecules seem to be stabilized in front of the methyl group through the formation C-H...O interactions. In addition, these structures provide the first observation of magnesium cations bound to the major groove of A-DNA and reveal two distinct modes of metal binding in methylated and native duplexes. These findings suggest that methylated cytosine bases could be recognized by protein or DNA polar residues through their tightly bound water molecules.
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Hydration and recognition of methylated CpG steps in DNA.,Mayer-Jung C, Moras D, Timsit Y EMBO J. 1998 May 1;17(9):2709-18. PMID:9564052<ref>PMID:9564052</ref>
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The line below this paragraph, containing "STRUCTURE_382d", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_382d| PDB=382d | SCENE= }}
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===HYDRATION AND RECOGNITION OF METHYLATED CPG STEPS IN DNA.===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_9564052}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 9564052 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_9564052}}
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==About this Structure==
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[[382d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=382D OCA].
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==Reference==
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<ref group="xtra">PMID:009564052</ref><references group="xtra"/>
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[[Category: Mayer-Jung, C.]]
[[Category: Mayer-Jung, C.]]
[[Category: Moras, D.]]
[[Category: Moras, D.]]

Revision as of 11:05, 14 May 2014

HYDRATION AND RECOGNITION OF METHYLATED CPG STEPS IN DNA.

382d, resolution 2.20Å

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