Abstract
Over the course of the past 30 yr, a multitude of calcium-binding proteins has been discovered that employ several unique structural motifs for calciumion binding. The first prominent family identified bound calcium via a helixloop-helix structural motif, and was coined the EF-hand binding motif, as it occurs between the E and F helices of carp parvalbumin (1). Today, the EF-hand calcium-binding family is ubiquitous, with members implicated in varied roles such as calcium signaling cell response and calcium storage. More recently, other calcium-binding motifs such as those found in annexin repeats (2), C2 domain proteins (3), and EGF domain proteins (4) have been identified. Table 1 summarizes the characteristic amino acid sequence properties of each of these domains as provided in the PROSITE protein motif recognition database (5).
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Weljie, A.M., Heringa, J. (2002). Exploring Familial Relationships Using Multiple Sequence Alignment. In: Vogel, H.J. (eds) Calcium-Binding Protein Protocols: Volume 2: Methods and Techniques. Methods in Molecular Biology™, vol 173. Springer, Totowa, NJ. https://doi.org/10.1385/1-59259-184-1:231
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