Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution

J Mol Biol. 1986 Jan 5;187(1):125-9. doi: 10.1016/0022-2836(86)90412-2.

Abstract

The solution conformation of rabbit liver Cd27+-metallothionein-2 was determined by nuclear magnetic resonance (n.m.r.) and distance geometry. The n.m.r. data are based on complete sequence-specific resonance assignments for the polypeptide chain. This letter describes the global arrangement of the polypeptide chain, which forms two distinct domains containing metal clusters of three and four Cd ions, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Liver / metabolism
  • Magnetic Resonance Spectroscopy
  • Metallothionein / metabolism*
  • Protein Conformation
  • Rabbits

Substances

  • Metallothionein