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Copper(II)-binding induces a unique polyproline type II helical structure within the ion-binding segment in the intrinsically disordered F-domain of ecdysteroid receptor from Aedes aegypti.
Autorzy
Rok wydania
2019
Czasopismo
Numer woluminu
58
Strony
11782-11792
DOI
10.1021/acs.inorgchem.9b01826
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
Reproduction of the dominant vector of Zika and dengue diseases, Aedes aegypti mosquito, is controlled by an active heterodimer complex composed of the 20-hydroxyecdysone receptor (EcR) and ultraspiracle protein. Although A. aegypti EcR shares the structural and functional organization with other nuclear receptors, its C-terminus has an additional long F domain (AaFEcR). Recently, we showed that the full length AaFEcR is intrinsically disordered with the ability to specifically bind divalent metal ions. Here, we describe the details of the exhaustive structural and thermodynamic properties of Zn2+- and Cu2+-complexes with the AaFEcR domain, based on peptide models of its two putative metal binding sites (Ac-HGPHPHPHG-NH2 and Ac-QQLTPNQQQHQQQHSQLQQVHANGS-NH2). Unexpectedly, only in the presence of increasing concentrations of Cu2+ ions, the Ac-HGPHPHPHG-NH2 peptide gained a metal ion-induced poly-l-proline type II helical structure, which is unique for members of the family of nuclear receptors.
Adres publiczny
http://dx.doi.org/10.1021/acs.inorgchem.9b01826
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The intrinsically disordered C-terminal F domain of the ecdysteroid receptor from Aedes aegypti exhibits metal ion-binding ability.
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