Artificial leucine rich repeats as new scaffolds for protein design

被引：6

作者：

Baabur-Cohen, Hemda ^{[1
]}

Dayalan, Subashini ^{[1
]}

Shumacher, Inbal ^{[1
]}

Cohen-Luria, Rivka ^{[1
]}

Ashkenasy, Gonen ^{[1
]}

机构：

[1] Ben Gurion Univ Negev, Dept Chem, Beer Sheva, Israel

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2011年 / 21卷 / 08期

关键词：

Leucine rich repeat proteins; Native chemical ligation; Peptides; Protein design; CONSENSUS DESIGN; INTERNALIN-B; LISTERIA; DOMAIN; RECOGNITION; STABILITY;

D O I：

10.1016/j.bmcl.2011.02.093

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The leucine rich repeat (LRR) motif that participates in many biomolecular recognition events in cells was suggested as a general scaffold for producing artificial receptors. We describe here the design and first total chemical synthesis of small LRR proteins, and their structural analysis. When evaluating the tertiary structure as a function of different number of repeating units (1-3), we were able to find that the 3-repeats sequence, containing 90 amino acids, folds into the expected structure. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：2372 / 2375

页数：4

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