1. Sequence reversed peptide from CaMKK binds to calmodulin in reversible Ca2+-dependent manner
- Author
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Isaac T. S. Li, Kevin Truong, and K.R. Ranjith
- Subjects
Models, Molecular ,animal structures ,Dependent manner ,Calmodulin ,Molecular Sequence Data ,Cell ,Biophysics ,Sequence (biology) ,Peptide ,Protein Serine-Threonine Kinases ,Biochemistry ,medicine ,Humans ,Amino Acid Sequence ,Protein kinase A ,Molecular Biology ,Peptide sequence ,chemistry.chemical_classification ,biology ,Kinase ,Cell Biology ,Peptide Fragments ,Protein Structure, Tertiary ,medicine.anatomical_structure ,chemistry ,biology.protein ,Calcium ,Protein Binding - 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.
- Published
- 2007