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Le domaine THAP de THAP1 : structure par RMN en solution et interaction avec l'ADN

Abstract : The THAP proteins family is characterised by the presence of a protein motif, designed the THAP domain, conserved during evolution and found in a thousand of human and model animal organism proteins. Human THAP1 protein is a regulator of the cell cycle through pRB/E2F pathway. The THAP domain of THAP1 is a C-X2-4-C-X35-50-C-X2-H type of zinc binding module with sequence specific DNA-binding properties. We solved the three-dimensional structure of the THAP domain of THAP1 by solution Nuclear Magnetic Resonance. This atypical zinc finger of ~ 80 residues is distinguished by the presence of a long ΒΑΒ motif between the two pairs of the C2CH zinc coordinating residues. We studied the DNA-binding of the THAP domain of THAP1 by the determination of a specific dissociation constant with Surface Plasmon Resonance studies and by performing chemical shift mapping in order to identify DNA-binding affected residues. Combining the chemical shift perturbation data with mutagenesis data allowed us to map the DNA-binding interface of the domain to a highly positively charged area and to build a DNA-protein interaction model showing an original way of recognition.
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Contributor : Damien Bessiere <>
Submitted on : Wednesday, February 20, 2008 - 11:53:32 AM
Last modification on : Thursday, October 15, 2020 - 9:57:19 AM
Long-term archiving on: : Thursday, May 20, 2010 - 6:45:29 PM


  • HAL Id : tel-00257781, version 1



Damien Bessiere. Le domaine THAP de THAP1 : structure par RMN en solution et interaction avec l'ADN. Biochimie [q-bio.BM]. Université Paul Sabatier - Toulouse III, 2008. Français. ⟨tel-00257781⟩



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