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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography	High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion Michela Bollati , Emanuele Scalone , Francesco Boni , Eloise Mastrangelo , Toni Giorgino , Mario Milani , Matteo De Rosa Biochemical And Biophysical Research Communications DOI: 10.1016/j.bbrc.2019.08.013 Diamond Proposal Number(s): [20221] Show Abstract ▼ Abstract: The second domain of gelsolin (G2) hosts mutations responsible for a hereditary form of amyloidosis. The active form of gelsolin is Ca2+-bound; it is also a dynamic protein, hence structural biologists often rely on the study of the isolated G2. However, the wild type G2 structure that have been used so far in comparative studies is bound to a crystallographic Cd2+, in lieu of the physiological calcium. Here, we report the wild type structure of G2 in complex with Ca2+ highlighting subtle ion-dependent differences. Previous findings on different G2 mutations are also briefly revised in light of these results.	Aug 2019
	Structure and functionality in flavivirus NS-proteins: Perspectives for drug design Michela Bollati , Karin Alvarez , Rene Assenberg , Cecile Baronti , Bruno Carnard , Shelley Cook , Bruno Coutard , Etienne Decroly , Xavier De Lamballerie , Ernest A. Gould , Gilda Grard , Jonathan Grimes , Rolf Hilgenfeld , Anna M. Jansson , Helene Malet , Erika Mancini , Eloise Mastrangelo , Andrea Mattevij , Mario Milani , David I. Stuart , Gregory Moureau , Johan Neyts , Raymond J. Owens , Jingshan Ren , Barbara Selisko , Silvia Speroni , Holger Steuber , Torsten Unge , Martino Bolognesi Antiviral Research DOI: 10.1016/j.antiviral.2009.11.009 Open Access Show Abstract ▼ Abstract: Flaviviridae are small enveloped viruses hosting a positive-sense single-stranded RNA genome. Besides yellow fever virus, a landmark case in the history of virology, members of the Flavivirus genus, such as West Nile virus and dengue virus, are increasingly gaining attention due to their re-emergence and incidence in different areas of the world. Additional environmental and demographic considerations suggest that novel or known flaviviruses will continue to emerge in the future. Nevertheless, up to few years ago flaviviruses were considered low interest candidates for drug design. At the start of the European Union VIZIER Project, in 2004, just two crystal structures of protein domains from the flaviviral replication machinery were known. Such pioneering studies, however, indicated the flaviviral replication complex as a promising target for the development of antiviral compounds. Here we review structural and functional aspects emerging from the characterization of two main components (NS3 and NS5 proteins) of the flavivirus replication complex. Most of the reviewed results were achieved within the European Union VIZIER Project, and cover topics that span from viral genomics to structural biology and inhibition mechanisms. The ultimate aim of the reported approaches is to shed light on the design and development of antiviral drug leads.	Nov 2009

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