News & Views

Yeast phosphorylase is regulated by phosphorylation. Details of the structure of the unphosphorylated, inactive enzyme suggest how the addition of a phosphate group activates the catalytic function of the protein.

The structure of the bovine mitochondrial F₁-ATPase lends further support to the idea that the enzyme generates ATP from a proton gradient by spinning like a top.

The structure of an intact colicin-la protein suggests that channel formation by this molecule may be more complex than previously suggested.

A clutch of recent lipase structures lifts the lid on the mechanism of interfacial activation and the determinants of lipase substrate specificity

The structure of two viral 3C cysteine proteinases confirm predictions of a close similarity with serine proteinases and hint at the evolutionary origins of this family of enzymes.

Insight into how Src Homology 3 domains interact with proline-rich ligands is provided by structures of Abl-SH3 with and without peptide and a Fyn-SH3/ligand complex.

The principle fold of the pleckstrin homology domain, found in a subset of cytoskeletal and signal transduction proteins, is now revealed and will inform and direct functional studies.

Recent structures of the DNA-bibding proteins E47 and MyoD provide new variations on the basic helix-loop-helix motif.

SH2 domains mediate protein-protein interactions and are involved in a wide range of intracellular signalling events, but what is the basis of their specificity?

By binding a peptide consisting of all D-amino acids calmodulin appears to have broken one of the central tenets of biochemistry; that protein interactions are stereospecific.

Knowledge of the structures of pharmacologically important proteins is having an ever incresing influence on the development of new drugs.

Three newly-determined structures testify to the widespread use of zinc for folding protein domains

Characterization of a family of RNA molecules selected in vitro to bind the L-valine side chain should shed light on nucleic acid-hydrophobic amino-acid interactions

An RNA structure prediction algorithm making use of phylogenetic and biochemical data propels RNA folding from two into three dimensions.

The structure of an uncleaved serpin reveals a number of unusual features that have important implications for the mechanism of serpin action.

The application of concepts derived from protein folding to the analysis of protein-DNA interactions provides the basis of an ‘induced fit’ model for sequence-specific DNA binding.

Photosynthesis, the foundation of life on earth, is slowly yielding up its secrets, as the structure of a light harvesting complex associated with photosystem II demonstrates.

The structure of the regulatory domain of scallop myosin at 2.8 Å resolution reveals secrets whose significance goes beyond the immediate implications for myosin-linked regulation.

The structure of the lectin and epidermal growth factor-related domains of E-selectin, an adhesion molecule involved with inflammation, provide further insight into selectin-carbohydrate interactions.