Abstract
The discovery of 2/2Hbs as short haemoproteins structurally related to haemoglobins, in the 1990s, was complemented by extensive sequence and crystallo-graphic investigations in the early 2000s. Amino acid sequences first provided a clear indication that the 2/2Hb family (formerly known as “truncated Hbs”) is composed of three main protein groups (I, II and III) that display low primary structure conservation relative to vertebrate Hbs. Crystal structures showed that a simple protein fold, essentially composed of four α-helices, is common to members of all three groups. Specific structural features can however be recognised in each 2/2Hb group. Among these, a tightly intertwined network of hydrogen bonds stabilising the heme exogenous ligand, based on group-specific distal site residues, is a landmark of all 2/2Hbs. We present here a review of the different structural aspects discovered for the 2/2Hb family, in the light of the currently known three-dimensional structures.
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Pesce, A., Milani, M., Nardini, M., Bolognesi, M. (2008). A Crystallographer’s Perspective on the 2/2Hb Family. In: Bolognesi, M., di Prisco, G., Verde, C. (eds) Dioxygen Binding and Sensing Proteins. Protein Reviews, vol 9. Springer, Milano. https://doi.org/10.1007/978-88-470-0807-6_4
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DOI: https://doi.org/10.1007/978-88-470-0807-6_4
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