Crystallization, characterization and measurement of MAD data on crystals of dengue virus NS3 serine protease complexed with mung-bean Bowman-Birk inhibitor.
Crystallization and preliminary characterization of the essential dengue virus NS3 serine protease complexed with a Bowman-Birk-type inhibitor from mung beans are reported. As the structure proved resistant to solution by molecular replacement and multiple isomorphous replacement methods, multi-wavelength anomalous diffraction data at the LIII edge of a holmium derivative have been measured. Promising Bijvoet and dispersive signals which are largely consistent with expected values have been extracted from the data. The structure, when determined, will provide a structural basis for the design, synthesis and evaluation of inhibitors of the protease for chemotherapy of dengue infections.
Center for Macromolecular Crystallography, University of Alabama at Birmingham, 79-THT, MCLM-244, 1918 University Boulevard, Birmingham, AL 35294-0005, USA. murthy@onyx.cmc.uab.edu
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Krishna Murthy
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Judge
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DeLucas
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Clum
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Padmanabhan
D003460:Crystallization; D018360:Crystallography, X-Ray; D003716:Dengue Virus / Q000201:enzymology*; D011487:Protein Conformation; D020365:RNA Helicases; D012697:Serine Endopeptidases; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000737:chemistry*; D017361:Viral Nonstructural Proteins / Q000737:chemistry*; D043583:Nucleoside-Triphosphatase; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases
D020365:RNA Helicases; D012697:Serine Endopeptidases; D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D017361:Viral Nonstructural Proteins; C060028:NS3 protein, flavivirus; D043583:Nucleoside-Triphosphatase; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases