Reviews & Analysis

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.

The rate of refolding of cytochrome c is very rapid in the absence of non-native interactions , which raises questions about the general significance of both the rates and intermediates of protein folding that are normally observed.

The structure of bi-functional thymidylate synthase-dihydrofolate reductase suggests that substrate may be channelled accross the surface of the protein between the two active sites.

Hhal methyltransferase, caught in the act of methylating a cytosine on a DNA substrate, reveals how the enzyme overcomes the problem of chemically modifying bases in the relatively inaccessible environment of the DNA duplex.

A wealth of prediction about the structure of spectrin has now been confirmed by the x-ray crystallographic analysis of a dimer of spectrin repeat units. The data provide a structural rationale for various haemolytic anaemias.

The common topology of the matrix metalloproteinase family, and details of the structures of individual members, will intensify efforts to develop drugs for diseases such as arthritis and cancer.

High-resolution structure analysis and directed mutagenesis experiments may at last be brought into step by the use of functional group analogues that alter individual atoms

Biochemical techniques provide a detailed picture of how the catalytic core of the Tetrahymena ribozyme interacts with the surface of its helical substrate.

To address important biological questions structural studies must be combined with quantitative methods of measurement and analysis derived from physics, chemistry and mathematics.