Evolution of Iron(II)-Finger Peptides by Using a Bipyridyl Amino Acid

被引：33

作者：

Kang, Mingchao ^{[1
]}

Light, Kenneth ^{[2
]}

Ai, Hui-wang ^{[1
]}

Shen, Weijun ^{[1
]}

Kim, Chan Hyuk ^{[1
]}

Chen, Peng R. ^{[1
]}

Lee, Hyun Soo ^{[1
]}

Solomon, Edward I. ^{[2
]}

Schultz, Peter G. ^{[1
]}

机构：

[1] Scripps Res Inst, Dept Chem, La Jolla, CA 92037 USA

[2] Stanford Univ, Dept Chem, Stanford, CA 94305 USA

来源：

CHEMBIOCHEM | 2014年 / 15卷 / 06期

关键词：

amino acids; bipyridyl complexes; iron; phage display; zinc finger engineering; IRON(III) HETEROLIGAND COMPLEXES; CRYSTAL-STRUCTURE DETERMINATION; MIXED-LIGAND COMPLEXES; ZINC FINGERS; DESIGN; SPECTRA; IRON; 2,2'-BIPYRIDINE; POLYPEPTIDE; REDUCTASE;

D O I：

10.1002/cbic.201300727

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 report the engineering of zinc-finger-like motifs containing the unnatural amino acid (2,2-bipyridin-5-yl)alanine (Bpy-Ala). A phage-display library was constructed in which five residues in the N-terminal finger of zif268 were randomized to include both canonical amino acids and Bpy-Ala. Panning of this library against a nine-base-pair DNA binding site identified several Bpy-Ala-containing functional Zif268 mutants. These mutants bind the Zif268 recognition site with affinities comparable to that of the wild-type protein. Further characterization indicated that the mutant fingers bind low-spin Fe-II rather than Zn-II. This work demonstrates that an expanded genetic code can lead to new metal ion binding motifs that can serve as structural, catalytic, or regulatory elements in proteins.

引用

页码：822 / 825

页数：4

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