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Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography

Authors :
Gonzalo Obal
X. Zhang
L. Tomé
Alejandro Buschiazzo
Otto Pritsch
Nicole Larrieux
Federico Carrión
Felipe Trajtenberg
Protein Biophysics [Montevideo] (UBP)
Institut Pasteur de Montevideo
Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)
Universidad de la República [Montevideo] (UDELAR)
Protein Crystallography / Cristalografía de Proteínas [Montevideo]
Virologie Structurale - Structural Virology
Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)
Département de Biologie structurale et Chimie - Department of Structural Biology and Chemistry
Institut Pasteur [Paris] (IP)
We acknowledge funding from Centre National de la Recherche Scientifique (France, program Laboratoire International Associé 316), Agencia Nacional de Investigación e Innovación (Uruguay), Centro de Biología Estructural del Mercosur (www.cebem.org.ar) and Fondo para la Convergencia Estructural del MERCOSUR (COF 03/11).
Universidad de la República [Montevideo] (UCUR)
Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)
Institut Pasteur [Paris]
Source :
Science, Science, 2015, 349 (6243), pp.95-98. ⟨10.1126/science.aaa5182⟩, Science, American Association for the Advancement of Science, 2015, 349 (6243), pp.95-98. ⟨10.1126/science.aaa5182⟩
Publication Year :
2015
Publisher :
HAL CCSD, 2015.

Abstract

Retroviral capsids in their native form Capsid proteins of retroviruses form protective lattices around viral RNA molecules. The precise molecular details of how individual, full-length capsid proteins assemble to shield the viral genome; however, are not well understood. Obal et al. and Gres et al. now report high resolution crystal structures of the full length capsid proteins from Bovine Leukemia Virus and HIV-1, respectively. The two studies complement each other to reveal the dynamic nature of capsid protein assembly and of how individual capsid proteins interact in the lattice. The findings may have relevance for drug design. Science , this issue p. 95 ; see also p. 99

Details

Language :
English
ISSN :
00368075 and 10959203
Database :
OpenAIRE
Journal :
Science, Science, 2015, 349 (6243), pp.95-98. ⟨10.1126/science.aaa5182⟩, Science, American Association for the Advancement of Science, 2015, 349 (6243), pp.95-98. ⟨10.1126/science.aaa5182⟩
Accession number :
edsair.doi.dedup.....8cdf796db6cf18c981cf6f8d8ef88625