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Analyses of the Alzheimer's disease β-amyloid peptide are revealing the chemical basis for its propensity to form insoluble neurotoxic fibrils and suggest an intriguing link between the free radical theory of neurodegenerative disorders and the chemistry of amyloidogenic peptides.
The first sighting of the ATP synthase ε subunit structure—a vital component of the stalk involved in energy transmission between membrane-bound and cytoplasmic portions of the synthase—provides intriguing hints about its possible mode of action.
Uteroglobin—a small, water soluble homodimeric protein possessing a large interior cavity—encloses a variety of endogenous and xenobiotic hydrophobic molecules. Although the structural results have mechanistic implications, the function of the protein remains speculative.
Low-temperature laser experiments provide insight into the rough energy landscape of myoglobin, strengthen the evidence for a hierarchical organization of the protein, and allow tantalizing glimpses into the dynamics of proteins.
In cytochrome c, the unfolding reaction occurs in four discreet stops, as monitored by the exchange of solvent hydrogen for backbone aminde hydrogens under varying denaturant concentrations.
Direct NMR observation of a transient folding intermediate provides new evidence for the importance of molten globules as general intermediates in protein folding.
Identification of the residues involved in the reaction catalysed by aldehyde reductase should aid in the development of drugs for the treatment of diabetic complications.
NMR structures of calmodulin, troponin C and related proteins are providing the atomic details of the conformational changes that transduce Ca2+ signals into mechanical or metabolic responses.
The structure of the apo form of calcyclin, a member of the S100 family of calcium-binding proteins, reveals a novel dimer fold that may reflect the presence of a new interface for target protein recognition.
Pleckstrin homology (PH) domains bind to membrane surfaces, and inositol phospholipids appear to form part of the binding sites. Recent structural studies provide a model for PH domain anchoring to inositol phospholipids that will open new avenues for functional investigation.
Dimeric proteins can arise from monomers by the simple exchange of secondary structural elements or a wholesale swapping of domains. These results have implications for the construction of novel oligomeric molecules and illuminate how existing structures may have evolved.
The structure of γδ resolvase complexed with a DNA cleavage site provides new insights into how resolvase accomplishes site-specific DNA recombination.
Structural analysis reveals mechanisms of drug resistance to HIV-1 protease inhibitors. These results have implications for the design of drugs and therapeutic strategies to combat drug resistance in AIDS.
Proteins that interact with RNA are now yielding to high-resolution structural analysis and these studies are going hand-in-hand with dissection of the RNA processing machinery of the spliceosome.
Examination of recent protein structures in the light of present views on the mechanism of protein folding provides clues as to events that may occur during the folding process.
A new structure of a plant lectin-saccharide complex shows how this protein presents a high density of sugar-binding sites. Comparison with other lectin structures reveals some emerging patterns in the arrangements of multiple ligand-binding sites in various lectin families.
Iterative protein structure-based ligand design has led to a ‘selective’ inhibitor of human non-pancreatic secretory phospholipase A2 which provides a new tool for probing metabolic pathways and may lead to a useful drug.
