Novel metal-binding proteins by design

Michael Klemba; Kevin H. Gardner; Stephen Marino; Neil D. Clarke; Lynne Regan

doi:10.1038/nsb0595-368

Novel metal-binding proteins by design

Michael Klemba, Kevin H. Gardner, Stephen Marino, Neil D. Clarke, Lynne Regan

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

93 Scopus citations

Abstract

We describe the successful design of a tetrahedral His₃Cys 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.

Original language	English (US)
Pages (from-to)	368-373
Number of pages	6
Journal	Nature Structural Biology
Volume	2
Issue number	5
DOIs	https://doi.org/10.1038/nsb0595-368
State	Published - May 1995

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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abstract = "We describe the successful design of a tetrahedral His3Cys 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.",

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AU - Gardner, Kevin H.

AU - Marino, Stephen

AU - Clarke, Neil D.

AU - Regan, Lynne

PY - 1995/5

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AB - We describe the successful design of a tetrahedral His3Cys 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.

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Novel metal-binding proteins by design

Abstract

ASJC Scopus subject areas

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