Počet záznamů: 1  

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

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    0538306 - ÚOCHB 2022 RIV GB eng J - Článek v odborném periodiku
    Zouharová, Monika - Vymětal, Jiří - Bednárová, Lucie - Vaněk, O. - Herman, P. - Vetýšková, Veronika - Poštulková, Klára - Lingstaadas, P. S. - Vondrášek, Jiří - Boušová, Kristýna
    Intrinsically disordered protein domain of human ameloblastin in synthetic fusion with calmodulin increases calmodulin stability and modulates its function.
    International Journal of Biological Macromolecules. Roč. 168, Jan 31 (2021), s. 1-12. ISSN 0141-8130. E-ISSN 1879-0003
    Výzkumná infrastruktura: e-INFRA CZ - 90140
    Institucionální podpora: RVO:61388963
    Klíčová slova: calmodulin * fusion protein * intrinsically disordered protein (IDP) * ameloblastin
    Obor OECD: Biochemistry and molecular biology
    Impakt faktor: 8.025, rok: 2021
    Způsob publikování: Omezený přístup
    https://doi.org/10.1016/j.ijbiomac.2020.11.216

    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.
    Trvalý link: http://hdl.handle.net/11104/0316306

     
     
Počet záznamů: 1  

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