Detail Structure of hepatitis C virus polymerase in complex with primer-template RNA (from Journal of Virology, 2012, 86 (12), 6503-6511) Bibliografi Author: Mosley, Ralph T. ; Edwards, Thomas E. ; Murakami, Eisuke ; Lam, Angela M. ; Grice, Rena L. ; Du, Jinfa ; Sofia, Michael J. ; Furman, Philip A. ; Otto, Michael J. Topik: HCV; RNA; Hepatitis - Cadangan Bahasa: (EN )     Penerbit: American Society for Microbiology     Tempat Terbit: Washington, D.C.    Tahun Terbit: 2012     Jenis: Article - diterbitkan di jurnal ilmiah internasional Fulltext: J. Virol.-2012-Mosley-6503-11.pdf (3.37MB; 0 download) [Informasi yang berkaitan dengan koleksi ini di internet] Abstract The replication of the hepatitis C viral (HCV) genome is accomplished by the NS5B RNA-dependent RNA polymerase (RdRp), for which mechanistic understanding and structure-guided drug design efforts have been hampered by its propensity to crystallize in a closed, polymerization-incompetent state. The removal of an autoinhibitory -hairpin loop from genotype 2a HCV NS5B increases de novo RNA synthesis by>100-fold, promotes RNA binding, and facilitated the determination of the first crystallographic structures of HCV polymerase in complex with RNA primer-template pairs. These crystal structures demonstrate the structural realignment required for primer-template recognition and elongation, provide new insights into HCV RNA synthesis at the molecular level, and may prove useful in the structure-based design of novel antiviral compounds. Additionally, our approach for obtaining the RNA primer-template-bound structure of HCV polymerase may be generally applicable to solving RNA-bound complexes for other viral RdRps that contain similar regulatory -hairpin loops, including bovine viral diarrhea virus, dengue virus, and West Nile virus. [hepatitis - cadangan] Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Lihat Sejarah Pengadaan  Konversi Metadata   Kembali

Copyright © 2006, 2007 Unika Atma Jaya, all rights reserved