Artificial leucine rich repeats as new scaffolds for protein design

Hemda Baabur-Cohen; Subashini Dayalan; Inbal Shumacher; Rivka Cohen-Luria; Gonen Ashkenasy

doi:10.1016/j.bmcl.2011.02.093

Artificial leucine rich repeats as new scaffolds for protein design

Hemda Baabur-Cohen, Subashini Dayalan, Inbal Shumacher, Rivka Cohen-Luria, Gonen Ashkenasy

Department of Chemistry

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

7 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	2372-2375
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	21
Issue number	8
DOIs	https://doi.org/10.1016/j.bmcl.2011.02.093
State	Published - 15 Apr 2011

Keywords

Leucine rich repeat proteins
Native chemical ligation
Peptides
Protein design

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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10.1016/j.bmcl.2011.02.093

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title = "Artificial leucine rich repeats as new scaffolds for protein design",

abstract = "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.",

keywords = "Leucine rich repeat proteins, Native chemical ligation, Peptides, Protein design",

author = "Hemda Baabur-Cohen and Subashini Dayalan and Inbal Shumacher and Rivka Cohen-Luria and Gonen Ashkenasy",

note = "Funding Information: This work was supported by a grant from the Israel–USA binational fund ( 2006358 ). The authors thank Dr. Dima Lukatsky with the help of I-TASSER modeling, and Prof. Yitzhak Tor (UCSD) for scientific discussions. ",

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AU - Baabur-Cohen, Hemda

AU - Dayalan, Subashini

AU - Shumacher, Inbal

AU - Cohen-Luria, Rivka

AU - Ashkenasy, Gonen

N1 - Funding Information: This work was supported by a grant from the Israel–USA binational fund ( 2006358 ). The authors thank Dr. Dima Lukatsky with the help of I-TASSER modeling, and Prof. Yitzhak Tor (UCSD) for scientific discussions.

PY - 2011/4/15

Y1 - 2011/4/15

N2 - 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.

AB - 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.

KW - Leucine rich repeat proteins

KW - Native chemical ligation

KW - Peptides

KW - Protein design

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JO - Bioorganic and Medicinal Chemistry Letters

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Artificial leucine rich repeats as new scaffolds for protein design

Abstract

Keywords

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