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384d

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{{STRUCTURE_384d| PDB=384d | SCENE= }}
{{STRUCTURE_384d| PDB=384d | SCENE= }}
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'''HYDRATION AND RECOGNITION OF METHYLATED CPG STEPS IN DNA'''
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===HYDRATION AND RECOGNITION OF METHYLATED CPG STEPS IN DNA===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 9564052 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9564052}}
==About this Structure==
==About this Structure==
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[[Category: Double helix]]
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[[Category: Modified]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:18:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:00:27 2008''

Revision as of 14:00, 27 July 2008

Image:384d.png

Template:STRUCTURE 384d

HYDRATION AND RECOGNITION OF METHYLATED CPG STEPS IN DNA

Template:ABSTRACT PUBMED 9564052

About this Structure

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 Sun Jul 27 17:00:27 2008

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