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Structural dynamics of picornaviral RdRP complexes. Implications for the design of antivirals

AutorVerdaguer, Núria ; Ferrer-Orta, Cristina ; Domingo, Esteban
Palabras claveRibavirin
RNA-dependent RNA polymerase
Replication fidelity
Picornavirus
Fecha de publicación2012
EditorSpringer
CitaciónMacromolecular Crystallography: 183-193 (2012)
SerieNATO Science for Peace and Security Series A: Chemistry and Biology 2012
ResumenGenome replication in picornavirus is catalyzed by a virally encoded RNA dependent RNA polymerase, termed 3D. These viruses also use a small protein primer, named VPg to initiate RNA replication. Polymerase 3D also catalyzes the covalent linkage of UMP to a N-terminal tyrosine on VPg. Seven different crystal structures of foot-and-mouth disease virus (FMDV) 3D catalytic complexes have enhanced our understanding of template and primer recognition, VPg uridylylation and rNTP binding and catalysis. In addition, the biochemical and structural analyses of six different FMDV 3D ribavirin resistant mutants provided evidences of three different mechanisms of resistance to this mutagenic nucleoside analogue. Such structural information is providing new insights into the fidelity of RNA replication, and for the design of antiviral compounds. © 2012 Springer Science+Business Media B.V.
URIhttp://hdl.handle.net/10261/88007
DOI10.1007/978-94-007-2530-0_17
Identificadoresdoi: 10.1007/978-94-007-2530-0_17
isbn: 978-94-007-2529-4
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