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Etudes fonctionnelles et structurales de la protéine EED, partenaire cellulaire du virus VIH-1 et de la cellulase « froide » Cel5G de Pseudoalteromonas haloplanktis

Abstract : The human protein EED belongs to the Polycomb Group. It acts as a transcriptional repressor and as a gene silencer. EED seems also to be important during the HIV-1 replication cycle, participating in the trafficking of preintegration complex and favouring the IN-mediated DNA integration reaction. EED has been overexpressed and purified in order to be crystallized alone or in complex with its viral partners IN, MA and Nef. A 3D structure model of EED has been obtained by homology modelling. Interaction regions determined by phage-display are localized on loops of the model.
The psychrophilic P. haloplanktis produces the cellulase Cel5G. Its crystallographic structure was solved alone and in complex with cellobiose by molecular replacement at 1.4 Å and 1.6 Å resolution, respectively. Cellulase Cel5A from the mesophilic E. chrysanthemi has been used as a search model. Structural details and comparisons give new insights into the understanding of aspects governing the cold adaptation of the enzyme at a molecular level.
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https://tel.archives-ouvertes.fr/tel-00091916
Contributor : Sébastien Violot <>
Submitted on : Thursday, September 7, 2006 - 3:38:16 PM
Last modification on : Thursday, November 21, 2019 - 2:35:35 AM
Long-term archiving on: : Monday, April 5, 2010 - 10:35:17 PM

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  • HAL Id : tel-00091916, version 1

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Sébastien Violot. Etudes fonctionnelles et structurales de la protéine EED, partenaire cellulaire du virus VIH-1 et de la cellulase « froide » Cel5G de Pseudoalteromonas haloplanktis. Biochimie [q-bio.BM]. Université Claude Bernard - Lyon I, 2005. Français. ⟨tel-00091916⟩

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