384d
From Proteopedia
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| - | [[Image:384d.gif|left|200px]] | + | [[Image:384d.gif|left|200px]] |
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| - | '''HYDRATION AND RECOGNITION OF METHYLATED CPG STEPS IN DNA''' | + | {{Structure |
| + | |PDB= 384d |SIZE=350|CAPTION= <scene name='initialview01'>384d</scene>, resolution 2.150Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HYDRATION AND RECOGNITION OF METHYLATED CPG STEPS IN DNA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 384D is a [ | + | 384D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=384D OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9564052 9564052] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Mayer-Jung, C.]] | [[Category: Mayer-Jung, C.]] | ||
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[[Category: modified]] | [[Category: modified]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:55:11 2008'' |
Revision as of 16:55, 20 March 2008
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| , resolution 2.150Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HYDRATION AND RECOGNITION OF METHYLATED CPG STEPS IN DNA
Overview
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.
About this Structure
384D is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 18:55:11 2008
Categories: Protein complex | Mayer-Jung, C. | Moras, D. | Timsit, Y. | MG | A-dna | Double helix | Modified
