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ETUDES STRUCTURALES ET FONCTIONNELLES
DE L'ATPASE-CA2+ DU RETICULUM SARCOPLASMIQUE (SERCA1A). EFFETS DES CONDITIONS DE CRISTALLISATION SUR LA CONFORMATION DE L'ATPASE-CA2+

Abstract : Sarcoplasmic reticulum Ca2+-ATPase is a membrane protein for which several conformations have been determined by X-ray crystallography. These structures have been very useful to guide interpretation of our functional studies of the role of the A domain and of the L6-7 loop in Ca2+-ATPase. However, we have shown that crystallization conditions may sometimes induce artefactual structures. Thus, the presence of high concentrations of Ca2+ during the crystallization process may favour for the AMPPCP-bound enzyme a structure different from the average one prevailing in solution. Similarly, inhibitors generally used to stabilize Ca2+-free ATPase close the access from the lumen to its Ca2+ binding sites in «E2P like» states. We have finally documented and attempted to understand both advantages and drawbacks to the use of amphipatic polymers for stabilisation of membrane proteins in solution.
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https://tel.archives-ouvertes.fr/tel-00011390
Contributor : Martin Picard <>
Submitted on : Monday, January 16, 2006 - 2:42:08 PM
Last modification on : Tuesday, December 8, 2020 - 3:42:32 AM
Long-term archiving on: : Friday, November 25, 2016 - 9:58:18 AM

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  • HAL Id : tel-00011390, version 1

Citation

Martin Picard. ETUDES STRUCTURALES ET FONCTIONNELLES
DE L'ATPASE-CA2+ DU RETICULUM SARCOPLASMIQUE (SERCA1A). EFFETS DES CONDITIONS DE CRISTALLISATION SUR LA CONFORMATION DE L'ATPASE-CA2+. Biochimie [q-bio.BM]. Université Pierre et Marie Curie - Paris VI, 2005. Français. ⟨tel-00011390⟩

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