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Bending and adaptability to proteins of the cAMP DNA-responsive element: molecular dynamics contrasted with NMR.

Abstract：

:DNA bending is assumed to play a crucial role during recognition of the cAMP-responsive element (CRE) by transcription factors. However, diverging results have been obtained for the bending direction of the unbound double helix. The refined NMR structures present a bend directed toward the minor groove, while biochemical methods conclude that there is a bend toward the major groove. The present 10-ns molecular dynamics (MD) simulation of d(GAGATGACGTCATCTC)(2), which contains the octamer CRE in its center, was carried out with AMBER in explicit water and counterions. It shows that CRE is a flexible segment, although it is bent slightly toward the major groove (7 degrees -8 degrees ) on the average. The MD structure agrees with both the biochemical results and unrefined NMR data. The divergence with the NMR refined structures suggests an improper electrostatic parameterization in the refinement software. The malleability of the central CpG is certainly the major contribution to the curving of the whole CRE segment in both the unbound and bound states. Comparison with the crystal structure of CRE bound to GCN4 shows that the deformation induced by the protein is concentrated mainly on the CpG step, rendering the bound structure of CRE closer to the structure of the 12-0 tetradecanoylphorbol-beta-acetate-responsive element.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Derreumaux S,Fermandjian S

doi

10.1016/S0006-3495(00)76324-7

subject

Has Abstract

pub_date

2000-08-01 00:00:00

pages

656-69

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(00)76324-7

journal_volume

79

pub_type

杂志文章

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