Induced-fit binding of a polyproline helix by a β-hairpin peptide

Dale J. Wilger; Jessica H. Park; Robert M. Hughes; Matthew E. Cuellar; Marcey L. Waters

doi:10.1002/anie.201106177

Induced-fit binding of a polyproline helix by a β-hairpin peptide

Dale J. Wilger, Jessica H. Park, Robert M. Hughes, Matthew E. Cuellar, Marcey L. Waters

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

11 Scopus citations

Abstract

Form-fitting: The study of a minimal mimic of a protein domain that binds to type II polyproline helices through an aromatic cleft is reported. This binding motif mimics that of protein domains, including those important in disease states such as HIV infection and cancer. This study provides insight into the structure-function relationship in binding as well as quantitative data on the magnitude of prolyl-π interactions relevant to inhibitor design.

Original language	English (US)
Pages (from-to)	12201-12204
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	50
Issue number	51
DOIs	https://doi.org/10.1002/anie.201106177
State	Published - Dec 16 2011
Externally published	Yes

Keywords

peptide structure
prolyl-π interaction
protein mimetics
protein-protein interactions
β hairpins

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/anie.201106177

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abstract = "Form-fitting: The study of a minimal mimic of a protein domain that binds to type II polyproline helices through an aromatic cleft is reported. This binding motif mimics that of protein domains, including those important in disease states such as HIV infection and cancer. This study provides insight into the structure-function relationship in binding as well as quantitative data on the magnitude of prolyl-π interactions relevant to inhibitor design.",

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AU - Park, Jessica H.

AU - Hughes, Robert M.

AU - Cuellar, Matthew E.

AU - Waters, Marcey L.

PY - 2011/12/16

Y1 - 2011/12/16

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AB - Form-fitting: The study of a minimal mimic of a protein domain that binds to type II polyproline helices through an aromatic cleft is reported. This binding motif mimics that of protein domains, including those important in disease states such as HIV infection and cancer. This study provides insight into the structure-function relationship in binding as well as quantitative data on the magnitude of prolyl-π interactions relevant to inhibitor design.

KW - peptide structure

KW - prolyl-π interaction

KW - protein mimetics

KW - protein-protein interactions

KW - β hairpins

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Induced-fit binding of a polyproline helix by a β-hairpin peptide

Abstract

Keywords

UN SDGs

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