Conformational flexibility of the dengue virus RNA - dependent RNA 1 polymerase revealed by a complex with an inhibitor 2 3

نویسندگان

  • Christian G. Noble
  • Siew Pheng Lim
  • Yen-Liang Chen
  • Chong Wai Liew
  • Julien Lescar
چکیده

Conformational flexibility of the dengue virus RNA-dependent RNA 1 polymerase revealed by a complex with an inhibitor 2 3 Christian G. Noble, Siew Pheng Lim, Yen-Liang Chen, Chong Wai Liew, Lijian 4 Yap, Julien Lescar *, and Pei-Yong Shi* 5 6 Novartis Institute for Tropical Diseases, 10 Biopolis Road, 05-01 Chromos, 7 School of Biological Sciences, Nanyang Technological University, Singapore 8 CNRS, AFMB UMR 7257, 13288, Marseille, France 9 10 11 12 *Corresponding authors: 13 Julien Lescar: School of Biological Sciences, Nanyang Technological University; 14 Phone: +65 65869706; Fax: +65; E-mail: [email protected] 15 Pei-Yong Shi: 10 Biopolis Road, 05-01, Chromos, Singapore 138670; Phone: +65 16 67222909; Fax: +65 67222916; E-mail: [email protected] 17 18 Running title: Dengue virus polymerase structure 19 20

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Conformational flexibility of the Dengue virus RNA-dependent RNA polymerase revealed by a complex with an inhibitor.

We report a highly reproducible method to crystallize the RNA-dependent RNA polymerase (RdRp) domain of dengue virus serotype 3 (DENV-3), allowing structure refinement to a 1.79-Å resolution and revealing amino acids not seen previously. We also present a DENV-3 polymerase/inhibitor cocrystal structure at a 2.1-Å resolution. The inhibitor binds to the RdRp as a dimer and causes conformational c...

متن کامل

NS3 helicase from dengue virus specifically recognizes viral RNA sequence to ensure optimal replication

The protein-RNA interactions within the flavivirus replication complex (RC) are not fully understood. Our structure of dengue virus NS3 adenosine triphosphatase (ATPase)/helicase bound to the conserved 5' genomic RNA 5'-AGUUGUUAGUCU-3' reveals that D290 and R538 make specific interactions with G2 and G5 bases respectively. We show that single-stranded 12-mer RNA stimulates ATPase activity of NS...

متن کامل

The effect of temperature on the binding affinity of Remdesivir and RdRp enzyme of SARS-COV-2 virus using steered molecular dynamics simulation

The fatal SARS-COV-2 virus appeared in China at the end of 2019 for the first time. This virus has similar sequence with SARS-COV in 2002, but its infection is very high rate. On the other hand, SARS-COV-2 is a RNA virus and requires RNA-dependent RNA polymerase (RdRp) to transcribe its viral genome. Due to the availability of the active site of this enzyme, an effective treatment is targeting ...

متن کامل

De novo synthesis of negative-strand RNA by Dengue virus RNA-dependent RNA polymerase in vitro: nucleotide, primer, and template parameters.

By using a purified dengue virus RNA-dependent RNA polymerase and a subgenomic 770-nucleotide RNA template, it was shown previously that the ratio of the de novo synthesis product to hairpin product formed was inversely proportional to increments of assay temperatures (20 to 40 degrees C). In this study, the components of the de novo preinitiation complex are defined as ATP, a high concentratio...

متن کامل

RNA sequences and structures required for the recruitment and activity of the dengue virus polymerase.

Dengue virus RNA-dependent RNA polymerase specifically binds to the viral genome by interacting with a promoter element known as stem-loop A (SLA). Although a great deal has been learned in recent years about the function of this promoter in dengue virus-infected cells, the molecular details that explain how the SLA interacts with the polymerase to promote viral RNA synthesis remain poorly unde...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2013