Abstract
In this chapter, we will continue to examine variations on themes in protein structure. We will reproduce using modern techniques the first multiple sequence alignment that was based upon three-dimensional protein structures. Then, we will look at the structure of an activated complex of the adrenaline receptor and a heterotrimeric G-protein and examine the tricks that were necessary to determine the structure. With an eye to the future, we will examine a structure of the human spliceosome complex that was determined by the increasingly powerful technique of cryo-electron microscopy. The chapter finishes by returning to the structure of hemoglobin, this time also determined by cryo-electron microscopy. Hemoglobin is at present the smallest structure determined by this method, but it seems likely to lose this attribute very soon.
“Three-dimensional alignment of the common nucleotide binding structure in dehydrogenases, kinases and flavodoxins permits the recognition of homologous amino acids when sequence comparisons alone would fail.” Michael Rossmann, Dino Moras and Kenneth Olsen (Rossmann et al. 1974)
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Skern, T. (2018). Moving from Former to Future Frontiers. In: Exploring Protein Structure: Principles and Practice. Learning Materials in Biosciences. Springer, Cham. https://doi.org/10.1007/978-3-319-76858-8_9
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