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Calcium-Binding Protein Protocols: Volume 2: Methods and Techniques pp 231–253Cite as

Exploring Familial Relationships Using Multiple Sequence Alignment

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Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 173))

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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Author information

Authors and Affiliations

  1. Department of Biological Sciences, University of Calgary, Calgary, AB, Canada

    Aalim M. Weljie

  2. Division of Mathematical Biology, MRC National Institute for Medical Research, London, UK

    Jaap Heringa

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  1. Aalim M. Weljie
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Editors and Affiliations

  1. Department of Biological Sciences, University of Calgary Calgary, AB, Canada

    Hans J. Vogel

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© 2002 Humana Press Inc.

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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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  • DOI: https://doi.org/10.1385/1-59259-184-1:231

  • Publisher Name: Springer, Totowa, NJ

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