Sequence reversed peptide from CaMKK binds to calmodulin in reversible Ca2+ -dependent manner |
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Authors: | Li Isaac T S Ranjith K R Truong Kevin |
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Institution: | Institute of Biomaterials and Biomedical Engineering, University of Toronto, 164 College Street, Toronto, Ont., Canada M5S 3G9. |
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Abstract: | Calmodulin (CaM) is a highly versatile Ca(2+) signaling transducer known to regulate over a hundred proteins. In this paper, we further demonstrate the versatility of CaM binding by showing that it binds to a synthetic peptide (revCKKp) made by reversing the amino acid sequence of the CaM-binding peptide (CKKp) from CaM-dependent protein kinase kinase (CaMKK) (residues 438-463). Sequence comparison between revCKKp and other CaM-binding peptides (CBPs) from the CaM target databank showed that revCKKp does not resemble any existing classes of CBPs, except CKKp M. Zhang, T. Yuan, Molecular mechanisms of calmodulin's functional versatility, Biochem. Cell Biol. 76 (1998) 313-323; S.W. Vetter, E. Leclerc, Novel aspects of calmodulin target recognition and activation, Eur. J. Biochem. 270 (2003) 404-414]. Furthermore, computational modeling showed that revCKKp could bind CaM in a similar manner to CKKp. Lastly, we experimentally showed that our synthetic revCKKp binds to CaM in a reversible Ca(2+)-dependent manner. |
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Keywords: | Calmodulin Sequence reverse Calmodulin-binding peptide Calmodulin-dependent protein kinase kinase Ca2+-dependent binding Protein modeling Calmodulin affinity chromatography |
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