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Structures determined by X-ray crystallography and NMR spectroscopy are averages, whereas many important biological functions require significant departure from the ‘average’ conformation.
The ultimate control over cellular energy is provided by a creatine kinase. The newly determined crystal structure of mitochondrial creatine kinase indicates a role in channelling components from mitochondria to cytoplasm.
The structure of beef heart cytochrome c oxidase has been determined. The structural information provides new insights into the mechanism of electron transfer-driven proton translocation. It does not explain why the eukaryotic form of the enzyme is so complex, with 13 different subunits.
Groups from around the world involved in protein tertiary structure classification and structure comparision met in Paris to discuss and compare, for the first time, existing classification schemes.
The structure of the N-terminal Ig-superfamily (IgSF) domain of NCAM has a high similarity with the intermediate set of Ig-like domains: the first domain of the vascular cell adhesion molecule (VCAM-1), the M5 domain in titin, and telokin.
The complex of Grb2-SH2 a BCR-Abl target peptide reveals that the peptide binds in a β-turn conformation; Trp 121 closes the binding site C-terminal to the phosphotyrosyl residue of the ligand and prevents it from assuming the expected extended conformation.
