Open AccessCysteine contributions to metal binding preference for Zn/Cd in the beta-domain of metallothionein
Author(s) -
ChiaChing Chang,
W. F. Liao,
P. C. Huang
Publication year - 1998
Publication title -
protein engineering design and selection
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.627
H-Index - 109
eISSN - 1741-0134
pISSN - 1741-0126
DOI - 10.1093/protein/11.1.41
Subject(s) - metallothionein , avidity , chemistry , metal , cysteine , binding energy , mndo , binding domain , metal ions in aqueous solution , beta (programming language) , crystallography , binding site , stereochemistry , zinc , biochemistry , molecule , biology , enzyme , genetics , physics , organic chemistry , nuclear physics , antibody , programming language , computer science
Previous studies showed that metals in the beta-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 beta-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.
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