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

J Mol Model. 2010 Mar;16(3):387-94. doi: 10.1007/s00894-009-0542-x. Epub 2009 Jul 16.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cluster Analysis
  • Hydrogen Bonding
  • Metallothionein / chemistry*
  • Metals / chemistry
  • Mice
  • Molecular Sequence Data
  • Organometallic Compounds / chemistry
  • Peptides / chemistry
  • Protein Structure, Secondary
  • Rats
  • Sequence Alignment
  • Time Factors


  • Metals
  • Organometallic Compounds
  • Peptides
  • Metallothionein