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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.
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.
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
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.