Abstract
Calmodulin (CaM) is a prototypical Ca2+-sensor protein that can control many important biological functions by binding to hundreds of target proteins. To gain insight into the versatility of CaM-target recognition, we have analyzed the complex structures for many types of CaM-binding peptides and some target proteins. In particular, some recently reported novel complex structures reveal that the versatile target binding of CaM is accommodated by its flexible domain arrangement and the malleability of its interfaces.
Keywords: Calcium, calmodulin, calmodulin-binding peptide, target-protein, calmodulin-target complex, myristoylation
Protein & Peptide Letters
Title: Protein-Peptide Interaction Studies Demonstrate the Versatility of Calmodulin Target Protein Binding
Volume: 13 Issue: 5
Author(s): Hiroaki Ishida and Hans J. Vogel
Affiliation:
Keywords: Calcium, calmodulin, calmodulin-binding peptide, target-protein, calmodulin-target complex, myristoylation
Abstract: Calmodulin (CaM) is a prototypical Ca2+-sensor protein that can control many important biological functions by binding to hundreds of target proteins. To gain insight into the versatility of CaM-target recognition, we have analyzed the complex structures for many types of CaM-binding peptides and some target proteins. In particular, some recently reported novel complex structures reveal that the versatile target binding of CaM is accommodated by its flexible domain arrangement and the malleability of its interfaces.
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Cite this article as:
Ishida Hiroaki and Vogel J. Hans, Protein-Peptide Interaction Studies Demonstrate the Versatility of Calmodulin Target Protein Binding, Protein & Peptide Letters 2006; 13 (5) . https://dx.doi.org/10.2174/092986606776819600
DOI https://dx.doi.org/10.2174/092986606776819600 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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