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Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases.
Visualizing ATP-dependent RNA translocation by the NS3 helicase from HCV.
Clinical targeting of HIV capsid protein with a long-acting small molecule
The small molecule GS-6207, which disrupts the function of the HIV capsid protein, shows potential as a long-acting therapeutic agent for the treatment and prevention of HIV infection.
Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6 dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose.
Structural, Biochemical, and Biophysical Characterization of Idelalisib Binding to Phosphoinositide 3-Kinase δ*
- J. R. Somoza, David Koditek, M. Mcgrath
- Biology, ChemistryThe Journal of Biological Chemistry
- 28 January 2015
The data show that idelalisib is a potent and selective inhibitor of the kinase activity of PI3Kδ, and a crystal structure of idELalisib bound to the p110δ subunit ofPI3K δ furthers the understanding of the binding interactions that confer the potency and selectivity of the compound.
Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus.
Compared with human HGPRTase, there are substantial differences between the active sites of these two homologs, suggesting that it will be possible to find compounds that selectively inhibit the parasite enzyme.
Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease.
- Stephanie X. Wang, K. Pandey, J. McKerrow
- Biology, MedicineProceedings of the National Academy of Sciences…
- 1 August 2006
The crystal structure of FP2 in complex with a protease inhibitor, cystatin, and mutagenesis data suggest a molecular basis for this unique mechanism by highlighting the functional role of two Tyr within FP2(nose) and a conserved Glu outside this motif.
The taste-active regions of monellin, a potently sweet protein.
The mutagenesis work suggests that at least four residues, located N-terminal to the alpha-helix, form part of a taste-active region of monellin, and there is evidence that a second region, formed by residues in the fourth and fifth beta-strands, may also be contributing to m onellin's activity.
Crystal structure of human cathepsin V.
A comparison of cathepsin V's active site with the active sites of related proteases revealed a number of differences, especially in the S2 and S3 subsites, that could be exploited in identifying specific cathePSin V inhibitors or in identifying inhibitors of other cysteine proteases that would be selective against cathebsin V.
Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex.
Order at the active site suggests that a high degree of flexibility may be inherent in the catalytic function of IMPDH, and may facilitate structure-based identification and design of compounds that specifically inhibit the parasite enzyme.