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We report here the crystal structure of the recombinant GP2 ectodomain of the lymphocytic choriomeningitis virus, the arenavirus type species, at 1.8-\u212b resolution. The structure shows the characteristic trimeric coiled coil present in class I viral fusion proteins, with a central stutter that allows a close structural alignment with most of the available structures of class I and III viral fusion proteins. The structure further shows a number of intrachain salt bridges stabilizing the postfusion hairpin conformation, one of which involves an aspartic acid that appears released from a critical interaction with the stable signal peptide upon low pH activation.<\/jats:p>","DOI":"10.1073\/pnas.1108910108","type":"journal-article","created":{"date-parts":[[2011,11,29]],"date-time":"2011-11-29T21:43:52Z","timestamp":1322603032000},"page":"19967-19972","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":115,"title":["X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformation"],"prefix":"10.1073","volume":"108","author":[{"given":"S\u00e9bastien","family":"Igonet","sequence":"first","affiliation":[{"name":"D\u00e9partement de Virologie, Unit\u00e9 de Virologie Structurale, Institut Pasteur, F-75724 Paris Cedex 15, France;"},{"name":"Centre National de la Recherche Scientifique, Unit\u00e9 de Recherche Associ\u00e9e 3015, F-75724 Paris Cedex 15, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie-Christine","family":"Vaney","sequence":"additional","affiliation":[{"name":"D\u00e9partement de Virologie, Unit\u00e9 de Virologie Structurale, Institut Pasteur, F-75724 Paris Cedex 15, France;"},{"name":"Centre National de la Recherche Scientifique, Unit\u00e9 de Recherche Associ\u00e9e 3015, F-75724 Paris Cedex 15, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Clemens","family":"Vonrhein","sequence":"additional","affiliation":[{"name":"Global Phasing Ltd., Cambridge CB3 0AX, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"G\u00e9rard","family":"Bricogne","sequence":"additional","affiliation":[{"name":"Global Phasing Ltd., Cambridge CB3 0AX, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Enrico A.","family":"Stura","sequence":"additional","affiliation":[{"name":"Commissariat \u00e0 l\u2019Energie Atomique Saclay, Service d\u2019Ing\u00e9nierie et d\u2019Etudes des Prot\u00e9ines, CE-Saclay F-91191 Gif-sur-Yvette Cedex, France; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hans","family":"Hengartner","sequence":"additional","affiliation":[{"name":"Institute of Experimental Immunology, University Hospital, CH 8557 Z\u00fcrich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruno","family":"Eschli","sequence":"additional","affiliation":[{"name":"Institute of Experimental Immunology, University Hospital, CH 8557 Z\u00fcrich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F\u00e9lix A.","family":"Rey","sequence":"additional","affiliation":[{"name":"D\u00e9partement de Virologie, Unit\u00e9 de Virologie Structurale, Institut Pasteur, F-75724 Paris Cedex 15, France;"},{"name":"Centre National de la Recherche Scientifique, Unit\u00e9 de Recherche Associ\u00e9e 3015, F-75724 Paris Cedex 15, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2011,11,28]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"e1000047","DOI":"10.1371\/journal.ppat.1000047","article-title":"Chapare virus, a newly discovered arenavirus isolated from a fatal hemorrhagic fever case in Bolivia","volume":"4","author":"Delgado S","year":"2008","unstructured":"S Delgado, et al., Chapare virus, a newly discovered arenavirus isolated from a fatal hemorrhagic fever case in Bolivia. 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Virology 164, 30\u201338 (1988).","journal-title":"Virology"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.virol.2005.08.030","article-title":"Genetic analysis of heptad-repeat regions in the G2 fusion subunit of the Junin arenavirus envelope glycoprotein","volume":"343","author":"York J","year":"2005","unstructured":"J York, SS Agnihothram, V Romanowski, JH Nunberg, Genetic analysis of heptad-repeat regions in the G2 fusion subunit of the Junin arenavirus envelope glycoprotein. 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