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The solution structure of HIV-1 Nef and mapping of its binding surface for the SH3 domain of a protein tyrosine kinase illustrates how the primate lentiviruses have tapped into host cell activation pathways.
The ATP–Mg2+–oxalate ternary complex of Escherichia coli phosphoenolpyruvate carboxykinase shows domain closure on substrate binding, adds a new fold to kinase structures and reveals the first syn conformation of a nucleotide complexed to a protein.
The determination of the three-dimensional structure of the Escherichia coli Lac represser by X-ray crystallography reveals much of the mechanism of action of this historically important molecule.
The first structure of a sea anemone potassium channel toxin reveals how a novel structural scaffold can be used to present key functional groups for channel blockade.
A linked, imazole/pyrrole minor-groove ligand has been shown to bind sequence specif icially to a 13 base-pair target sequence in a mixed 1:1/2:1 mode.
