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rdf:type |
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lifeskim:mentions |
umls-concept:C0006072,
umls-concept:C0012854,
umls-concept:C0033618,
umls-concept:C0033684,
umls-concept:C0332307,
umls-concept:C0441712,
umls-concept:C0524637,
umls-concept:C0596957,
umls-concept:C1145667,
umls-concept:C1167622,
umls-concept:C1280500,
umls-concept:C1521840,
umls-concept:C1880497,
umls-concept:C1996904,
umls-concept:C2349209,
umls-concept:C2603343,
umls-concept:C2825311
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pubmed:issue |
4
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pubmed:dateCreated |
2005-9-29
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pubmed:abstractText |
Molecular dynamics simulations of a total duration of 30 ns in explicit solvent were carried out on the BPV-1-E2 protein complexed to a high-affinity DNA target containing the two hydrogen-bonded ACCG.CGGT half-sites separated by the noncontacted ACGT sequence. The analysis of the trajectories focuses on the DNA structure and on the dynamics. The data are compared to those issued from recent simulations made on three free targets that recognize E2 with different affinities. E2 does not drastically perturb the mechanic properties of the free DNA: the structural relationships between the BI/BII backbone substates and some helical parameters are preserved in the complex despite a severe slowing down of the phosphate group motions. The structures of both free and bound half-sites are very close to each other although the conformational space explored by these regions is narrowed when they are contacted by the protein. The enhanced plasticity found in the best free target spacers, mainly manifested through the backbone motions, allows a clear overlap between several free and bound global DNA features such as the base displacement. Furthermore, this flexibility is preserved in the complex. Our results support the hypothesis that E2 takes advantage of free predistorted structures that may minimize the DNA deformation cost. In addition, we observe that E2 is far from totally stiffening the DNA, suggesting that the entropic penalty inherent in the complex formation could be limited.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-10194299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-10217454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-10512722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-10672034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-10906136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-11099379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-11423431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-11601858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-11988474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-12162959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-12384592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-12445784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-12548619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-12548627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-12595561,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-12683994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-12744707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-12888343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-12930964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-1328886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-14755572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-15001352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-15027032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-15048770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-15148366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-15165850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-15326025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-2026600,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-2144453,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-2154890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-2482765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-2536165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-2542129,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-2714249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-2850174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-7174662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-8011939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-8441668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-8985322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-9500925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16055534-9500927
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2542-51
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16055534-Base Sequence,
pubmed-meshheading:16055534-Binding Sites,
pubmed-meshheading:16055534-Computer Simulation,
pubmed-meshheading:16055534-DNA,
pubmed-meshheading:16055534-DNA-Binding Proteins,
pubmed-meshheading:16055534-Models, Chemical,
pubmed-meshheading:16055534-Models, Molecular,
pubmed-meshheading:16055534-Molecular Sequence Data,
pubmed-meshheading:16055534-Motion,
pubmed-meshheading:16055534-Protein Binding,
pubmed-meshheading:16055534-Protein Conformation,
pubmed-meshheading:16055534-Structure-Activity Relationship,
pubmed-meshheading:16055534-Viral Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Molecular dynamics studies on free and bound targets of the bovine papillomavirus type I e2 protein: the protein binding effect on DNA and the recognition mechanism.
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pubmed:affiliation |
Laboratoire de Biochimie Théorique, CNRS UPR 9080, Institut de Biologie Physico-chimique, Paris, France. djuranov@ibpc.fr
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pubmed:publicationType |
Journal Article
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