Cysteine contributions to metal binding preference for Zn/Cd in the β-domain of metallothionein

Chia Ching Chang, Wen Fa Liao, P C Huang

Research output: Contribution to journalArticle

Abstract

Previous studies showed that metals in the β-domain of metallothionein (MT) are more readily exchangeable and the level of avidity is site specific. This is reflected by energy differences computed with a series of simulated structures derived from X-ray crystallography. In this study, we examined further the contribution of each of the nine cysteines in the β-domain. By semi-empirical MNDO calculations, we observed that the relative average binding strength is the strongest for Cys21 to Cd[M4] and for Cys26 to Zn[M3], except for the bridging cysteines. These results suggest that binding site preference for Zn/Cd is determined by binding strength between specific cysteines and metal ion species.

Original languageEnglish (US)
Pages (from-to)41-46
Number of pages6
JournalProtein Engineering
Volume11
Issue number1
StatePublished - Jan 1998

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Metallothionein
X ray crystallography
Binding sites
Metal ions
Cysteine
Metals
X Ray Crystallography
Binding Sites
Ions

Keywords

  • Binding energy
  • Metallothionein
  • MNDO
  • Quantum

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry

Cite this

Cysteine contributions to metal binding preference for Zn/Cd in the β-domain of metallothionein. / Chang, Chia Ching; Liao, Wen Fa; Huang, P C.

In: Protein Engineering, Vol. 11, No. 1, 01.1998, p. 41-46.

Research output: Contribution to journalArticle

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