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Structural Biology 2018
Volume: 4
Biochemistry & Molecular Biology Journal
Page 48
March 15-16 2018
Barcelona, Spain
10
th
Edition of International Conference on
Structural Biology
T
he proteins of the dengue virus are expressed as a single
polyprotein, which is then processed proteolytically into
individual functional fragments by proteases from both the host
and the virus itself. The viral protease is the N-terminal domain
of the non-structural protein 3 (NS3pro) and is an attractive
target for drug-based therapeutic intervention. NS3pro by itself
is expressed in the inclusion bodies and requires a 47-residue
hydrophilic region of the non-structural protein 2B (NS2B) for its
correct folding and enzymatic activity. As NS2B is flexible and
dynamic, existing crystal structures are unable to give a complete
picture of the NS2B-NS3pro complex for drug development.
A method inspired by a recent paper was used for the partial
isotopic labelling of the NS2B-NS3pro complex, which simplifies
the multidimensional spectra obtained through nuclear magnetic
resonance (NMR) experiments. We aim to find out how the
dynamics of NS2B contributes towards the proteolytic activity
of the dengue virus NS3pro, through various NMR dynamics
experiments. Relaxation dispersion data reveal that theC-terminal
portion of NS2B unfolds itself around 4% of the time. Mutants
of NS2B were generated to explore how both the dynamics and
protease activity change with the mutations.
Biography
Kenneth Lee is currently doing his PhD in the Department of Biological Sci-
ences, of the National University of Singapore. He is expecting to complete
his PhD in 2018.
dbsydw@nus.edu.sgInvestigating the role of NS2B dynamics in dengue virus NS3
protease function
Kenneth Lee
and
Daiwen Yang
National University of Singapore, Singapore
Kenneth Lee et al., Biochem Mol biol J, Volume 4
DOI: 10.21767/2471-8084-C1-009