Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy

Barbara A. Messerle*, Andreas Schäffer, Milan Vašák, Jeremias H R Kägi, Kurt Wüthrich

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

154 Citations (Scopus)


The three-dimensional structure of human [113Cd7]metallothionein-2 was determined by nuclear magnetic resonance spectroscopy in solution. Sequence-specific 1H resonance assignments were obtained using the sequential assignment method. The input for the structure calculations consisted of the metal-cysteine co-ordinative bonds identified with heteronuclear correlation spectroscopy, 1H-1H distance constraints from nuclear Overhauser enhancement spectroscopy, and spin-spin coupling constants 3JHNαand3Jαβ. The molecule consists of two domains, the β-domain including amino acid residues 1 to 30 and three metal ions, and the α-domain including residues 31 to 61 and four metal ions. The nuclear magnetic resonance data present no evidence for a preferred relative orientation of the two domains. The polypeptide-to-metal co-ordinative bonds in human metallothionein-2 are identical to those in the previously determined solution structures of rat metallothionein-2 and rabbit metallothionein-2a, and the polypeptide conformations in the three proteins are also closely similar.

Original languageEnglish
Pages (from-to)765-779
Number of pages15
JournalJournal of molecular biology
Issue number3
Publication statusPublished - 5 Aug 1990
Externally publishedYes


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