Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker

Cited 19 time in webofscience Cited 17 time in scopus
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dc.contributor.authorJeong, Woo Hyeonko
dc.contributor.authorLee, Haerimko
dc.contributor.authorSong, Dong Hyunko
dc.contributor.authorEom, Jae-Hoonko
dc.contributor.authorKim, Sun Changko
dc.contributor.authorLee, Hee Seungko
dc.contributor.authorLee, Hayyoungko
dc.contributor.authorLee, Jie-Ohko
dc.date.accessioned2016-06-29T02:06:23Z-
dc.date.available2016-06-29T02:06:23Z-
dc.date.created2016-02-12-
dc.date.created2016-02-12-
dc.date.issued2016-05-
dc.identifier.citationNATURE COMMUNICATIONS, v.7-
dc.identifier.issn2041-1723-
dc.identifier.urihttp://hdl.handle.net/10203/208494-
dc.description.abstractBuilding a sophisticated protein nano-assembly requires a method for linking protein components in a predictable and stable structure. Most of the cross linkers available have flexible spacers. Because of this, the linked hybrids have significant structural flexibility and the relative structure between their two components is largely unpredictable. Here we describe a method of connecting two proteins via a 'fusion a helix' formed by joining two pre-existing helices into a single extended helix. Because simple ligation of two helices does not guarantee the formation of a continuous helix, we used EY-CBS, a synthetic cross linker that has been shown to react selectively with cysteines in a-helices, to stabilize the connecting helix. Formation and stabilization of the fusion helix was confirmed by determining the crystal structures of the fusion proteins with and without bound EY-CBS. Our method should be widely applicable for linking protein building blocks to generate predictable structures.-
dc.languageEnglish-
dc.publisherNATURE PUBLISHING GROUP-
dc.titleConnecting two proteins using a fusion alpha helix stabilized by a chemical cross linker-
dc.typeArticle-
dc.identifier.wosid000372194500001-
dc.identifier.scopusid2-s2.0-84979695436-
dc.type.rimsART-
dc.citation.volume7-
dc.citation.publicationnameNATURE COMMUNICATIONS-
dc.identifier.doi10.1038/ncomms11031-
dc.contributor.localauthorKim, Sun Chang-
dc.contributor.localauthorLee, Hee Seung-
dc.contributor.localauthorLee, Jie-Oh-
dc.contributor.nonIdAuthorLee, Hayyoung-
dc.description.isOpenAccessY-
dc.type.journalArticleArticle-
dc.subject.keywordPlusHYBRID COORDINATION MOTIFS-
dc.subject.keywordPlusSTRUCTURAL BASIS-
dc.subject.keywordPlusMOLECULAR RECOGNITION-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusBINDING-PROTEINS-
dc.subject.keywordPlusRECEPTOR-
dc.subject.keywordPlusPEPTIDE-
dc.subject.keywordPlusDESIGN-
dc.subject.keywordPlusRESOLUTION-
dc.subject.keywordPlusINTERFACES-
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