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The three-dimensional structure of the bacterial virus MS2
The structure of the icosahedral bacteriophage MS2 has been determined by X-ray crystallography and the coat protein has no structural similarity to that of any other known RNA virus. Expand
Structure and functionality in flavivirus NS-proteins: Perspectives for drug design
Structural and functional aspects emerging from the characterization of two main components (NS3 and NS5 proteins) of the flavivirus replication complex are reviewed to shed light on the design and development of antiviral drug leads. Expand
Structure and Function of Carbonic Anhydrases from Mycobacterium tuberculosis*
The structures of two of the three β-class carbonic anhydrases that have been identified in Mycobacterium tuberculosis are described, i.e. Rv1284 and Rv3588c, which exhibit both of the metal coordination geometries that have previously been observed for structures in this family. Expand
Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1.
It was found that disorder in the handle domain affects the formation and configuration of the tetradecamer and results in condensed structures with larger equatorial pores when compared with ClpPs from other species. Expand
Two-carbon-elongated HIV-1 protease inhibitors with a tertiary-alcohol-containing transition-state mimic.
A new generation of HIV-1 protease inhibitors encompassing a tertiary-alcohol-based transition-state mimic has been developed. By elongation of the core structure of recently reported inhibitors withExpand
Antiviral strategies to control calicivirus infections
An overview of the mechanisms underlying calicivirus infection is provided, focusing on the molecular aspects of replication in the host cell, and antiviral strategies that may significantly impact on the epidemiological characteristics of these highly successful viral pathogens are proposed. Expand
Structural basis for the inhibitory efficacy of efavirenz (DMP-266), MSC194 and PNU142721 towards the HIV-1 RT K103N mutant.
Structural observations from Efavirenz in complex with wild-type protein and the K103N mutant and PNU142721 and MSC194 in complex for HIV-1 RT indicate that the K 103N substitution induces only minor positional adjustments of the three inhibitors and the residues lining the binding pocket, which is consistent with the proposal. Expand
Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site.
It is demonstrated that the RpiB from Mycobacterium tuberculosis has catalytic properties very similar to those previously reported for the Escherichia coli RPIB enzyme, and the structure of the mycobacterial enzyme is reported, solved by molecular replacement and refined to 1.88A resolution. Expand
Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor.
Two cyclic, C2-symmetric HIV-1 protease inhibitors, one sulfamide and one urea derivative, both comprising phenyl ether groups in the P1/P1' positions, were cocrystallized with HIV-1 protease, andExpand
Structures of Mycobacterium tuberculosis 1-Deoxy-D-xylulose-5-phosphate Reductoisomerase Provide New Insights into Catalysis*
Structural information complemented with molecular dynamics simulations and free energy calculations provides the framework for the design of new inhibitors and gives new insights into the reaction mechanism. Expand