Tham khảo tài liệu 'báo cáo hóa học: " structural comparisons of the nucleoprotein from three negative strand rna virus families"', luận văn - báo cáo phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả | Virology Journal BioMed Central Hypothesis Open Access Structural comparisons of the nucleoprotein from three negative strand RNA virus families Ming Luo Todd J Green Xin Zhang Jun Tsao and Shihong Qiu Address Department of Microbiology University of Alabama at Birmingham Birmingham AL 35294 USA Email Ming Luo - mingluo@ Todd J Green - tgreen@ Xin Zhang - xinzhang@ Jun Tsao - juntsao@ Shihong Qiu - qiu@ Corresponding author Published 10 July 2007 Received 18 May 2007 Accepted 10 July 2007 Virology Journal 2007 4 72 doi 1743-422X-4-72 This article is available from http content 4 1 72 2007 Luo et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Structures of the nucleoprotein of three negative strand RNA virus families borna disease virus rhabdovirus and influenza A virus are now available. Structural comparisons showed that the topology of the RNA binding region from the three proteins is very similar. The RNA was shown to fit into a cavity formed by the two distinct domains of the RNA binding region in the rhabdovirus nucleoprotein. Two helices connecting the two domains characterize the center of the cavity. The nucleoproteins contain at least 5 conserved helices in the N-terminal domain and 3 conserved helices in the C-terminal domain. Since all negative strand RNA viruses are required to have the ribonucleoprotein complex as their active genomic templates it is perceivable that the 5H 3H structure is a common motif in the nucleoprotein of negative strand RNA viruses. Background Negative strand RNA viruses are different from all other viruses because their RNA genomes are always enwrapped by a virally coded nucleoprotein N to form a ribonucleoprotein
