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Influence of NH-S gamma bonding interactions on the structure and dynamics of metallothioneins


Romero-Isart, N; Oliva, B; Vašák, M (2010). Influence of NH-S gamma bonding interactions on the structure and dynamics of metallothioneins. Journal of Molecular Modeling, 16(3):387-394.

Abstract

Mammalian metallothioneins ([Formula: see text]) show a clustered arrangement of the metal ions and a nonregular protein structure. The solution structures of Cd(3)-thiolate cluster containing beta-domain of mouse beta-MT-1 and rat beta-MT-2 show high structural similarities, but widely differing structure dynamics. Molecular dynamics simulations revealed a substantially increased number of NH-Sgamma hydrogen bonds in beta-MT-2, features likely responsible for the increased stability of the Cd(3)-thiolate cluster and the enfolding protein domain. Alterations in the NH-Sgamma hydrogen-bonding network may provide a rationale for the differences in dynamic properties encountered in the beta-domains of MT-1, -2, and -3 isoforms, believed to be essential for their different biological function.

Abstract

Mammalian metallothioneins ([Formula: see text]) show a clustered arrangement of the metal ions and a nonregular protein structure. The solution structures of Cd(3)-thiolate cluster containing beta-domain of mouse beta-MT-1 and rat beta-MT-2 show high structural similarities, but widely differing structure dynamics. Molecular dynamics simulations revealed a substantially increased number of NH-Sgamma hydrogen bonds in beta-MT-2, features likely responsible for the increased stability of the Cd(3)-thiolate cluster and the enfolding protein domain. Alterations in the NH-Sgamma hydrogen-bonding network may provide a rationale for the differences in dynamic properties encountered in the beta-domains of MT-1, -2, and -3 isoforms, believed to be essential for their different biological function.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:March 2010
Deposited On:06 Jul 2010 17:39
Last Modified:21 Nov 2017 14:53
Publisher:Springer
ISSN:0948-5023
Publisher DOI:https://doi.org/10.1007/s00894-009-0542-x
PubMed ID:19609577

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