Structure-fonction of nucleoproteic complexes of DNA topoisomerases
Subgroup Leader : Valerie LAMOUR
Teams : Regulation of DNA topology
Our research group focuses on the molecular mechanisms governing nucleic acid transport, processing and topological changes of chromatin DNA. Our present targets are nucleoprotein complexes involved in retroviral DNA integration and eukaryotic DNA topoisomerases. We integrate structural data from high resolution (X-ray crystallography), medium resolution (CryoEM) and low resolution (cell imaging) with in vitro and in cellulo functional data.
The main focus of Marc Ruff is to understand the molecular processes performed by the HIV pre-integration complexes (PIC). The aim is to provide a four dimensional view of the PIC, from reverse transcription until integration. A second component of the project focuses on drug design aspects to optimize protein-protein interaction and conformational inhibitors.
Valérie Lamour’s project is aiming at the functional and structural studies of DNA topoisomerase cellular complexes targeted by therapeutic compounds used in cancer and anti-bacterial therapies. The main goal of this study is to identify and study the structure/function of Topoisomerase-associated complexes targeted by drugs through a combination of functional and structural approaches.
Subgroup Leader : Valerie LAMOUR
Teams : Regulation of DNA topology
Subgroup Leader : Nicolas LEVY
Teams : Regulation of DNA topology
Marlène Vayssières, postdoc
Léa Haas, engineer
Christophe Lotz, PhD student
Arnaud Vanden Broeck, PhD student
Claire Bedez, PhD student
Acta crystallographica Section D : Structural biology [1993-...] ; Volume: 55 ; Page: 721-723
Cell ; Volume: 94 ; Page: 239-249
Proteins - Structure, Function and Bioinformatics ; Volume: 25 ; Page: 139-141
Acta crystallographica Section D : Structural biology [1993-...] ; Volume: 52 ; Page: 211-214
Nature ; Volume: 375 ; Page: 377-382
Structural Tools for the Analysis of Protein-nucleic Acid Complexes ; Page: 287-298
Structure and Function. Vol. 2: Proteins ; Page: 159-168
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