Abstract
Calcium performs a unique role in biology, achieving biological effects through highly specific interactions with and modulation of target proteins1. It has been proposed that calcium-modulated proteins possess a characteristic, evolutionarily related, binding fold, known as the EF-hand2. The high-resolution X-ray structure of α-lactalbumin reveals a Ca2+ binding fold that resembles an EF-hand only superficially and presumably has no evolutionary relationship with it. However, there is clear homology with the corresponding loop in c-type lysozyme (the ‘parent’ molecule of α-lactalbumin). This study, at 1.7 Å resolution, represents one of the most accurate analyses of a calcium binding protein yet reported.
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Stuart, D., Acharya, K., Walker, N. et al. α-Lactalbumin possesses a novel calcium binding loop. Nature 324, 84–87 (1986). https://doi.org/10.1038/324084a0
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DOI: https://doi.org/10.1038/324084a0
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