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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Main Authors: 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
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0092513&type=printable
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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
collection DOAJ
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
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institution OA Journals
issn 1932-6203
language English
publishDate 2014-01-01
publisher Public Library of Science (PLoS)
record_format Article
series PLoS ONE
spelling doaj-art-a2d3722fb48247248b0db2e254f5bea72025-08-20T02:14:54ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0194e9251310.1371/journal.pone.0092513Computational design of binding proteins to EGFR domain II.Yoon Sup ChoiSoomin YoonKyung-Lock KimJiho YooParkyong SongMinsoo KimYoung-Eun ShinWon Jun YangJung-eun NohHyun-Soo ChoSanguk KimJunho ChungSung Ho RyuWe 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.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0092513&type=printable
spellingShingle 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.
PLoS ONE
title 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_short Computational design of binding proteins to EGFR domain II.
title_sort computational design of binding proteins to egfr domain ii
url https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0092513&type=printable
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