TY - JOUR AU - Salaemae, Wanisa AU - Junaid, Muhammad AU - Angsuthanasombat, Chanan AU - Katzenmeier, Gerd PY - 2010 DA - 2010/08/24 TI - Structure-guided mutagenesis of active site residues in the dengue virus two-component protease NS2B-NS3 JO - Journal of Biomedical Science SP - 68 VL - 17 IS - 1 AB - The dengue virus two-component protease NS2B/NS3 mediates processing of the viral polyprotein precursor and is therefore an important determinant of virus replication. The enzyme is now intensively studied with a view to the structure-based development of antiviral inhibitors. Although 3-dimensional structures have now been elucidated for a number of flaviviral proteases, enzyme-substrate interactions are characterized only to a limited extend. The high selectivity of the dengue virus protease for the polyprotein precursor offers the distinct advantage of designing inhibitors with exquisite specificity for the viral enzyme. To identify important determinants of substrate binding and catalysis in the active site of the dengue virus NS3 protease, nine residues, L115, D129, G133, T134, Y150, G151, N152, S163 and I165, located within the S1 and S2 pockets of the enzyme were targeted by alanine substitution mutagenesis and effects on enzyme activity were fluorometrically assayed. SN - 1423-0127 UR - https://doi.org/10.1186/1423-0127-17-68 DO - 10.1186/1423-0127-17-68 ID - Salaemae2010 ER -