Morgenstern Kurt A

TL;DR: The 2.5 angstrom resolution X-ray crystal structure of the NS3 protease domain complexed with a synthetic NS4A activator peptide is reported, which shows a chymotrypsin-like fold and features a tetrahedrally coordinated metal ion distal to the active site.

TL;DR: The structure of the HCV NS3 RNA helicase domain complexed with a single-stranded DNA oligonucleotide has been solved to 2.2 A resolution and is a member of a superfamily of helicases, termed superfamily II.

TL;DR: High-resolution crystal structures of an activated Lck kinase domain in complex with three structurally distinct ATP-competitive inhibitors demonstrate that kinase selectivity can be achieved with small-molecule inhibitors that exploit subtle topological differences among protein kinases.

TL;DR: This result suggests that NS4A does not change the pKa values of the active site residues of NS3 protease, and shows a marked catalytic preference for the cysteine residue commonly found in authentic substrates.

TL;DR: It is suggested that the domains within NS3 may influence the activity of one another and that the interplay of HCV genomic elements may regulate the enzyme activities of this complex HCV replicase component.