Reviews & Analysis

Inhibitor binding to HIV protease affects and can be affected by protein motions. Knowledge of these motions will be of considerable importance for effective structure-based design of drugs.

Crystal structures of the p50 subunit of transcription factor NF-κB bound to DNA reveal the remarkable way the protein uses loops to recognize DNA and how it presents a surface for interaction with other factors.

The difficult task of providing an atomic-level picture of integrin adhesion is beginning to bear fruit with the determination of the crystal structure of an α-chain sub-domain that has primary ligand-binding epitopes.

Replacement of a buried salt bridge by a hydrophobic cluster in the Arc repressor dimer sheds light on the role of ionic and hydrophobic interactions in proteins.

The structure of the catalytic domain of HIV integrase reveals a similarity with other proteins involved in DNA recombination or RNA degradation. Knowledge of the structure may help in the search for inhibitors of HIV replication.

A structure prediction challenge on a previously unprecedented scale has put the various protein fold recognition methodologies to the test.

The crystal structure of the PurR-DNA complex reveals how α-helices can be used for minor groove recognition and provides a model for the Lad family of repressors.

Determination of the pK_a values of the γ-phosphate in p21^ras mutants provides the first experimental evidence for substrate-assisted catalysis in the intrinsic GTPase reaction.

The structure of infinite networks of the carbohydarate-binding protein galectin-1 in complex with branched oligosaccharides is a major step towards understanding how this class of protein acts on cells.

Understanding how the cellular protein folding machinery works has taken a major step forward with the determination of the structure of the chaperonin GroEL

The first detailed look at the atomic structure of the hammerhead ribozyme provides a wealth of RNA structural information.

New structures of SH3 domains complexed with proline-rich peptides show that the ligands can bind in two opposite orientations; this feature has not been seen before in protein/protein recognition.

Structural studies of carbonmonoxy myoglobin photolyzed at ultra-low temperatures have allowed the visualization of an otherwise elusive binding intermediate.

As investigations into the structure and function of the PH domain intensify there are no shortage of clues as to the role of this domain in signal transduction, and yet the physiological ligand remains elusive.

Synthetic peptides are providing important insights into the nature and specificity of the G-protein α/effector interactions.

The explosion in determination of protein structures is now being mirrored by the all-important consideration of their motions.

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