113Cd NMR study of a metallothionein fragment. Evidence for a two-domain structure.

Y. Boulanger, I. M. Armitage, K. A. Miklossy, D. R. Winge

Research output: Contribution to journalArticle

78 Scopus citations

Abstract

A 32-residue polypeptide fragment, designated alpha I, of rat liver metallothionein obtained by subtilisin digestion was studied by 113Cd NMR. The amino acid composition of the fragment corresponded to residues 30-61 of the metallothionein primary structure, and it contained 3.4 g atoms of Cd2+/mol of alpha I-fragment. Four 113Cd resonances were observed, three of which had identical chemical shifts to those assigned to the four-metal cluster in human liver metallothionein-2 under the same pH and buffer conditions. The 5-ppm chemical shift difference between the remaining resonance assigned to the four-metal cluster in the intact protein can be explained to result from the removal of the NH2-terminal polypeptide fragment containing the three-metal cluster. These results provide unambiguous evidence for the two-domain structure of metallothionein, containing a separate three- and a four-metal cluster.

Original languageEnglish (US)
Pages (from-to)13717-13719
Number of pages3
JournalJournal of Biological Chemistry
Volume257
Issue number22
StatePublished - Nov 25 1982

Fingerprint Dive into the research topics of '113Cd NMR study of a metallothionein fragment. Evidence for a two-domain structure.'. Together they form a unique fingerprint.

  • Cite this

    Boulanger, Y., Armitage, I. M., Miklossy, K. A., & Winge, D. R. (1982). 113Cd NMR study of a metallothionein fragment. Evidence for a two-domain structure. Journal of Biological Chemistry, 257(22), 13717-13719.