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Institut de minéralogie, de physique des matériaux et de cosmochimie
UMR 7590 - Sorbonne Université/CNRS/MNHN/IRD

Structure and dynamics of signalling proteins

Group Leader: Pr. Catherine Vénien-Bryan

Many signals in the cell are conveyed by interacting protein molecules. How do protein-protein interactions lead to a response? The most likely explanation is through changes in structure. We study protein-protein interactions in the control of signalling processes using cryo-electron microscopy and combining the results with information from X-ray diffraction and biophysical studies.


Ion Channels

The regulation of the flow of potassium ions into cells is

important in the propagation of the neuronal action potential, cell volume regulation and muscle contraction. Potassium channels are controlled by pore gating : the channel can exist in either an open or a closed state. Our research is focused on understanding the intimate relationship between ion channel structure and function. The objective is to understand the molecular mechanism at an atomic level.

We are focusing on the inwardly-rectifying family of potassium channels or ‘Kir’ channels, more precisely Kirbac3.1 channel but also the eucaryotic Kir2.1 channel.

Genome integrity

Genome integrity is maintained with various DNA repair pathways. At the center of the DNA damage Fanconi Anemia repair pathway is the FANCD2/FANCI complex.

We are using cryo electron microscopy and image analysis for studying this complex machinary. Using a combination of molecular biology, cell biology, biochemistry and structural biology, we have identified the fork-like tower domain in the C-terminus of FANCD2 which is required for its complete functions in the DNA interstrand cross-link repair. Interestingly, several disease-causing mutations lie within this region, underscoring the importance of this domain. (collaboration Dr M Cohn, University of Oxford)

The CRACAM robot: Two-dimensional crystallization of membrane protein

Membrane proteins are key cellular components that perform essential functions. They are major therapeutic targets. Electron crystallography can provide structural experimental information at atomic scale for membrane proteins forming two-dimensional crystals. We have created a fully automated robot called CRACAM which is able to produce 2D crystals of membrane proteins either directly in the bulk of the solution or under a lipid monolayer at the air:water interface. This robot is versatile and canbe used also for immobilising various macromolecules at the air-water interface.



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Traductions :

    Zoom Science - Amorpheus : un logiciel en libre accès pour l’analyse des données de diffusion de rayons X sur des systèmes liquides ou amorphes

    L’étude de la structure locale d’un liquide ou d’un solide amorphe soumis à des conditions extrêmes de pression et de température permet d’en déduire la densité, ainsi que la compressibilité, l’expansion thermique et, éventuellement, d’identifier des transitions de phase liquide-liquide. L’analyse et...

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    A. Marco Saitta

    Directeur de l'institut



    Bruno Moal

    Secrétaire général

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    Jérôme Normand

    Gestion du personnel

    Réservation des salles



    Antonella Intili

    Accueil et logistique

    Réservation des salles



    Ouafa Faouzi

    Gestion financière (gestionimpmc @


    Cécile Duflot



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    Adresse postale

    Institut de minéralogie, de physique des matériaux et de cosmochimie - UMR 7590

    Sorbonne Université - 4, place Jussieu - BC 115 - 75252 Paris Cedex 5


    Adresse physique

    Institut de minéralogie, de physique des matériaux et de cosmochimie - UMR 7590 - Sorbonne Université - 4, place Jussieu - Tour 23 - Barre 22-23, 4e étage - 75252 Paris Cedex 5


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    Accès : 7 quai Saint Bernard - 75005 Paris, Tour 22.

    Contact : Antonella Intili : Barre 22-23, 4e étage, pièce 420, 33 +1 44 27 25 61



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