Computational design of binding proteins to EGFR domain II.

We developed a process to produce novel interactions between two previously unrelated proteins. This process selects protein scaffolds and designs protein interfaces that bind to a surface patch of interest on a target protein. Scaffolds with shapes complementary to the target surface patch were scr...

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Autores principales:	Yoon Sup Choi, Soomin Yoon, Kyung-Lock Kim, Jiho Yoo, Parkyong Song, Minsoo Kim, Young-Eun Shin, Won Jun Yang, Jung-eun Noh, Hyun-Soo Cho, Sanguk Kim, Junho Chung, Sung Ho Ryu
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a2d3722fb48247248b0db2e254f5bea7
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spelling	oai:doaj.org-article:a2d3722fb48247248b0db2e254f5bea72021-11-18T08:24:35ZComputational design of binding proteins to EGFR domain II.1932-620310.1371/journal.pone.0092513https://doaj.org/article/a2d3722fb48247248b0db2e254f5bea72014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24710267/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203We developed a process to produce novel interactions between two previously unrelated proteins. This process selects protein scaffolds and designs protein interfaces that bind to a surface patch of interest on a target protein. Scaffolds with shapes complementary to the target surface patch were screened using an exhaustive computational search of the human proteome and optimized by directed evolution using phage display. This method was applied to successfully design scaffolds that bind to epidermal growth factor receptor (EGFR) domain II, the interface of EGFR dimerization, with high reactivity toward the target surface patch of EGFR domain II. One potential application of these tailor-made protein interactions is the development of therapeutic agents against specific protein targets.Yoon Sup ChoiSoomin YoonKyung-Lock KimJiho YooParkyong SongMinsoo KimYoung-Eun ShinWon Jun YangJung-eun NohHyun-Soo ChoSanguk KimJunho ChungSung Ho RyuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 4, p e92513 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yoon Sup Choi Soomin Yoon Kyung-Lock Kim Jiho Yoo Parkyong Song Minsoo Kim Young-Eun Shin Won Jun Yang Jung-eun Noh Hyun-Soo Cho Sanguk Kim Junho Chung Sung Ho Ryu Computational design of binding proteins to EGFR domain II.
description	We developed a process to produce novel interactions between two previously unrelated proteins. This process selects protein scaffolds and designs protein interfaces that bind to a surface patch of interest on a target protein. Scaffolds with shapes complementary to the target surface patch were screened using an exhaustive computational search of the human proteome and optimized by directed evolution using phage display. This method was applied to successfully design scaffolds that bind to epidermal growth factor receptor (EGFR) domain II, the interface of EGFR dimerization, with high reactivity toward the target surface patch of EGFR domain II. One potential application of these tailor-made protein interactions is the development of therapeutic agents against specific protein targets.
format	article
author	Yoon Sup Choi Soomin Yoon Kyung-Lock Kim Jiho Yoo Parkyong Song Minsoo Kim Young-Eun Shin Won Jun Yang Jung-eun Noh Hyun-Soo Cho Sanguk Kim Junho Chung Sung Ho Ryu
author_facet	Yoon Sup Choi Soomin Yoon Kyung-Lock Kim Jiho Yoo Parkyong Song Minsoo Kim Young-Eun Shin Won Jun Yang Jung-eun Noh Hyun-Soo Cho Sanguk Kim Junho Chung Sung Ho Ryu
author_sort	Yoon Sup Choi
title	Computational design of binding proteins to EGFR domain II.
title_short	Computational design of binding proteins to EGFR domain II.
title_full	Computational design of binding proteins to EGFR domain II.
title_fullStr	Computational design of binding proteins to EGFR domain II.
title_full_unstemmed	Computational design of binding proteins to EGFR domain II.
title_sort	computational design of binding proteins to egfr domain ii.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/a2d3722fb48247248b0db2e254f5bea7
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_version_	1718421820250521600

Computational design of binding proteins to EGFR domain II.

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