NOVEL METAL-BINDING PROTEINS BY DESIGN

被引：88

作者：

KLEMBA, M

GARDNER, KH

MARINO, S

CLARKE, ND

REGAN, L

机构：

[1] YALE UNIV,DEPT MOLEC BIOPHYS & BIOCHEM,NEW HAVEN,CT 06520

[2] JOHNS HOPKINS UNIV,DEPT BIOPHYS,BALTIMORE,MD 21205

来源：

NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 05期

关键词：

D O I：

10.1038/nsb0595-368

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We describe the successful design of a tetrahedral His(3)Cys Zn(II)-binding site in a small protein of known structure: the B1 domain of Streptococcal protein G. The B1 variants containing the novel metal-binding site were characterized using a combination of optical absorption, circular dichroism and NMR spectroscopies. The results indicate that the designed proteins bind Zn(II) with high affinity and tetrahedral coordination geometry, and that the overall secondary and tertiary structure of the B1 domain is maintained.

引用

页码：368 / 373

页数：6

共 31 条

[1] KINETIC-ANALYSIS OF FOLDING AND UNFOLDING THE 56-AMINO ACID IGG-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN-G [J].