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Recent NMR structures of bovine immunodeficiency viral TAR RNA–Tat peptide complexes have revealed a new β-hairpin RNA recognition motif. These complexes exhibit intriguing new variations on the recurring themes in nucleic acid recognition.
Rubisco's CO2 cofactor is involved in divalent -metal binding, activity regulation and probably also in the catalytic chemistry. Recent studies of the CO2- and metal-binding site in the absence of phosphorylated ligands provide a structural understanding of the unusual activation mechanism.
The difference in amino-acid sequence and inferred molecular mechanisms between the pair of EF-hands in BM-40 and those of other EF-hand proteins force us to reconsider the evolutionary and functional relationships among the members of this diverse family of proteins.
Human aspartylglucosaminidase belongs to the newly recognized structural superfamily of Ntn aminohydrolases, which are characterized by the use of the side chain of the N-terminal amino acid as the nucleophile in catalysis.
The new refinement of GroEL sharpens the boundary between known and unknown regions of the structure, and raises questions about the treatment of ambiguity in structure determination.
Protein tyrosine phosphatases (PTPs) are a family of signal transduction enzymes that dephosphorylate phosphotyrosine containing proteins. Structural and kinetic studies provide a molecular understanding of how these enzymes regulate a wide range of intracellular processes.
New structures of copper containing proteins with cupredoxin-like folds confirm earlier predictions, and reveal electron-transfer routes in cytochrome oxidase, while a new fold for amine-oxidase reveals a new use for copper in forming self-derived quino-cofactor.
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.
