383d
From Proteopedia
(Difference between revisions)
m (Protected "383d" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | + | ==Hydration and recognition of methylated CPG steps in DNA== | |
| - | + | <StructureSection load='383d' size='340' side='right' caption='[[383d]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[383d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=383D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=383D FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene></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=383d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=383d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=383d RCSB], [http://www.ebi.ac.uk/pdbsum/383d PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Mayer-Jung, C | + | == References == |
| - | [[Category: Moras, D | + | <references/> |
| - | [[Category: Timsit, Y | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Mayer-Jung, C]] | ||
| + | [[Category: Moras, D]] | ||
| + | [[Category: Timsit, Y]] | ||
[[Category: A-dna]] | [[Category: A-dna]] | ||
[[Category: Dna]] | [[Category: Dna]] | ||
[[Category: Double helix]] | [[Category: Double helix]] | ||
[[Category: Modified deoxyribonucleic acid]] | [[Category: Modified deoxyribonucleic acid]] | ||
Revision as of 14:09, 18 December 2014
Hydration and recognition of methylated CPG steps in DNA
| |||||||||||
