作者: David S Booth , Yifan Cheng , Alan D Frankel
DOI: 10.7554/ELIFE.04121
关键词:
摘要: The HIV Rev protein routes viral RNAs containing the Response Element (RRE) through Crm1 nuclear export pathway to cytoplasm where proteins are expressed and genomic RNA is delivered assembling virions. RRE assembles a oligomer that displays sequences (NESs) for recognition by Crm1-Ran(GTP) receptor complex. Here we provide first view of an assembled HIV-host complex using single-particle electron microscopy. Unexpectedly, forms dimer with extensive interface enhances association Rev-RRE poises NES binding sites interact oligomer. between monomers explains differences orthologs alter determine cellular tropism replication. arrangement identifies novel surface possibly target inhibitor may point broader role dimerization in regulating host gene expression.