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Influence of $$ {\text{NH - }}{{\text{S}}^\gamma } $$ bonding interactions on the structure and dynamics of metallothioneins

Romero-Isart, Núria ; Oliva, Baldo ; Vašák, Milan

In: Journal of Molecular Modeling, 2010, vol. 16, no. 3, p. 387-394

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    Titre
    • Influence of $$ {\text{NH - }}{{\text{S}}^\gamma } $$ bonding interactions on the structure and dynamics of metallothioneins
    Auteur
    • Romero-Isart, Núria. Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057, Zürich, Switzerland
    • Oliva, Baldo. Structural Bioinformatics Lab. (GRIB) Barcelona Research Park of Biomedicine (PRBB), Universitat Pompeu Fabra-IMIM, 08003, Barcelona, Catalonia, Spain
    • Vašák, Milan. Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057, Zürich, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Journal of Molecular Modeling, 2010, vol. 16, no. 3, p. 387-394. Springer-Verlag
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:320563
    Summary
    Mammalian metallothioneins ($$ {\text{M}}_7^{\text{IIMTs}} $$) show a clustered arrangement of the metal ions and a nonregular protein structure. The solution structures of Cd3-thiolate cluster containing β-domain of mouse β-MT-1 and rat β-MT-2 show high structural similarities, but widely differing structure dynamics. Molecular dynamics simulations revealed a substantially increased number of $$ {\text{NH - }}{{\text{S}}^\gamma } $$ hydrogen bonds in β-MT-2, features likely responsible for the increased stability of the Cd3-thiolate cluster and the enfolding protein domain. Alterations in the $$ {\text{NH - }}{{\text{S}}^\gamma } $$ hydrogen-bonding network may provide a rationale for the differences in dynamic properties encountered in the β-domains of MT-1, -2, and -3 isoforms, believed to be essential for their different biological function