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Intrinsically disordered protein domain of human ameloblastin in synthetic fusion with calmodulin increases calmodulin stability and modulates its function

M. Zouharova, J. Vymetal, L. Bednarova, O. Vanek, P. Herman, V. Vetyskova, K. Postulkova, PS. Lingstaadas, J. Vondrasek, K. Bousova

. 2021 ; 168 (-) : 1-12. [pub] 20201205

Jazyk angličtina Země Nizozemsko

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc21019392

Constantly increasing attention to bioengineered proteins has led to the rapid development of new functional targets. Here we present the biophysical and functional characteristics of the newly designed CaM/AMBN-Ct fusion protein. The two-domain artificial target consists of calmodulin (CaM) and ameloblastin C-terminus (AMBN-Ct). CaM as a well-characterized calcium ions (Ca2+) binding protein offers plenty of options in terms of Ca2+ detection in biomedicine and biotechnologies. Highly negatively charged AMBN-Ct belongs to intrinsically disordered proteins (IDPs). CaM/AMBN-Ct was designed to open new ways of communication synergies between the domains with potential functional improvement. The character and function of CaM/AMBN-Ct were explored by biophysical and molecular modelling methods. Experimental studies have revealed increased stability and preserved CaM/AMBN-Ct function. The results of molecular dynamic simulations (MDs) outlined different interface patterns between the domains with potential allosteric communication within the fusion.

Citace poskytuje Crossref.org

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$a Zouharova, Monika $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 160 00 Prague, Czech Republic; Second Faculty of Medicine, Charles University, 150 06 Prague, Czech Republic
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$a Constantly increasing attention to bioengineered proteins has led to the rapid development of new functional targets. Here we present the biophysical and functional characteristics of the newly designed CaM/AMBN-Ct fusion protein. The two-domain artificial target consists of calmodulin (CaM) and ameloblastin C-terminus (AMBN-Ct). CaM as a well-characterized calcium ions (Ca2+) binding protein offers plenty of options in terms of Ca2+ detection in biomedicine and biotechnologies. Highly negatively charged AMBN-Ct belongs to intrinsically disordered proteins (IDPs). CaM/AMBN-Ct was designed to open new ways of communication synergies between the domains with potential functional improvement. The character and function of CaM/AMBN-Ct were explored by biophysical and molecular modelling methods. Experimental studies have revealed increased stability and preserved CaM/AMBN-Ct function. The results of molecular dynamic simulations (MDs) outlined different interface patterns between the domains with potential allosteric communication within the fusion.
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$a Vymetal, Jiri $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 160 00 Prague, Czech Republic
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$a Bednarova, Lucie $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 160 00 Prague, Czech Republic
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$a Vanek, Ondrej $u Department of Biochemistry, Faculty of Science, Charles University, 128 40 Prague, Czech Republic
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$a Herman, Petr $u Faculty of Mathematics and Physics, Charles University, 121 16 Prague, Czech Republic
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$a Vetyskova, Veronika $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 160 00 Prague, Czech Republic; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, 166 28 Prague, Czech Republic
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$a Postulkova, Klara $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 160 00 Prague, Czech Republic; Second Faculty of Medicine, Charles University, 150 06 Prague, Czech Republic
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$a Lingstaadas, Petter S $u Institute of Clinical Dentistry, University of Oslo, 0317 Oslo, Norway
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$a Vondrasek, Jiri $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 160 00 Prague, Czech Republic
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$a Bousova, Kristyna $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, 160 00 Prague, Czech Republic. Electronic address: kristyna.bousova@uochb.cas.cz
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