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

Werner Braun; Gerhard Wagner; Erich Wörgötter; Milan Vašák; Jeremias H.R. Kägi; Kurt Wüthrich

doi:10.1016/0022-2836(86)90412-2

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

Werner Braun, Gerhard Wagner, Erich Wörgötter, Milan Vašák, Jeremias H.R. Kägi, Kurt Wüthrich

Research output: Contribution to journal › Article › peer-review

124 Scopus citations

Abstract

The solution conformation of rabbit liver Cd₇²⁺-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.

Original language	English (US)
Pages (from-to)	125-129
Number of pages	5
Journal	Journal of Molecular Biology
Volume	187
Issue number	1
DOIs	https://doi.org/10.1016/0022-2836(86)90412-2
State	Published - Jan 5 1986
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Biophysics
Structural Biology

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10.1016/0022-2836(86)90412-2

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abstract = "The solution conformation of rabbit liver Cd72+-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.",

author = "Werner Braun and Gerhard Wagner and Erich W{\"o}rg{\"o}tter and Milan Va{\v s}{\'a}k and K{\"a}gi, {Jeremias H.R.} and Kurt W{\"u}thrich",

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AU - Braun, Werner

AU - Wagner, Gerhard

AU - Wörgötter, Erich

AU - Vašák, Milan

AU - Kägi, Jeremias H.R.

AU - Wüthrich, Kurt

PY - 1986/1/5

Y1 - 1986/1/5

N2 - The solution conformation of rabbit liver Cd72+-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.

AB - The solution conformation of rabbit liver Cd72+-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.

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

Abstract

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