Article
A crystal structure of the dengue virus non-structural protein 5 (NS5) polymerase delineates interdomain amino acid residues that enhance its thermostability and de novo initiation activities.
The Journal of biological chemistry - 25 Oct 2013
Lim Siew Pheng, Koh Jolene Hong Kiew, Seh Cheah Chen, Liew Chong Wai, Davidson Andrew D, Chua Leng Shiew, Chandrasekaran Ramya, Cornvik Tobias C, Shi Pei-Yong, Lescar Julien
Abstract excerpt
The dengue virus (DENV) non-structural protein 5 (NS5) comprises an N-terminal methyltransferase and a C-terminal RNA-dependent RNA polymerase (RdRp) domain. Both enzymatic activities form attractive targets for antiviral development. Available crystal structures of NS5 fragments indicate that residues 263-271 (using the DENV serotype 3 numbering) located between the two globular domains of NS5 could be flexible....
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