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Calmodulin Target Database

  • Published:
Journal of Structural and Functional Genomics

Abstract

The intracellular calcium sensor protein calmodulin (CaM) interacts with a large number of proteins to regulate their biological functions in response to calcium stimulus. This molecular recognition process is diverse in its mechanism, but can be grouped into several classes based on structural and sequence information. We have developed a web-based database (http://calcium.uhnres.utoronto.ca/ctdb) for this family of proteins containing CaM binding sites or, as we propose to call it herein, CaM recruitment signaling (CRS) motifs. At present the CRS motif found in approximately 180 protein sequences in the databases can be divided into four subclasses, each subclass representing a distinct structural mode of molecular recognition involving CaM. The database can predict a putative CRS location within a given protein sequence, identify the subclass to which it may belong, and structural and biophysical parameters such as hydrophobicity, hydrophobic moment, and propensity for a -helix formation.

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Authors and Affiliations

  1. Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ontario, M5G 2M9, Canada

    Kyoko L. Yap, Justin Kim, Kevin Truong, Marc Sherman & Tao Yuan

  2. Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ontario, M5G 2M9, Canada

    Mitsuhiko Ikura

Authors
  1. Kyoko L. Yap
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  2. Justin Kim
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  3. Kevin Truong
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  4. Marc Sherman
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  5. Tao Yuan
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  6. Mitsuhiko Ikura
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Yap, K.L., Kim, J., Truong, K. et al. Calmodulin Target Database. J Struct Func Genom 1, 8–14 (2000). https://doi.org/10.1023/A:1011320027914

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  • DOI: https://doi.org/10.1023/A:1011320027914

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