Selection of a buried salt bridge by phage display

被引：5

作者：

Vagt, Toni ^{[1
]}

Jaeckel, Christian ^{[1
]}

Samsonov, Sergey ^{[2
]}

Pisabarro, M. Teresa ^{[2
]}

Koksch, Beate ^{[1
]}

机构：

[1] Free Univ Berlin, Dept Biol Chem & Pharm, Inst Chem & Biochem, D-14195 Berlin, Germany

[2] TU Dresden Struct Bioinformat, BIOTEC, D-01307 Dresden, Germany

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2009年 / 19卷 / 14期

关键词：

Phage display; alpha-Helical coiled coil; Molecular dynamics; Protein design; ZINC-FINGER DOMAINS; COILED-COILS; SPECIFICITY; RECOGNITION; PEPTIDES; FLUORINE; DESIGN;

D O I：

10.1016/j.bmcl.2009.03.062

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The alpha-helical coiled coil is a valuable folding motif for protein design and engineering. By means of phage display technology, we selected a capable binding partner for one strand of a coiled coil bearing a charged amino acid in a central hydrophobic core position. This procedure resulted in a novel coiled coil pair featuring an opposed Glu-Lys pair arranged staggered within the hydrophobic core of a coiled coil structure. Structural investigation of the selected coiled coil dimer by CD spectroscopy and MD simulations suggest that a buried salt bridge within the hydrophobic core enables the specific dimerization of two peptides. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：3924 / 3927

页数：4

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