dc.contributor.author | Bryan, Allen W. | |
dc.contributor.author | Starner-Kreinbrink, Jennifer L. | |
dc.contributor.author | Hosur, Raghavendra | |
dc.contributor.author | Clark, Patricia L. | |
dc.contributor.author | Berger, Bonnie | |
dc.date.accessioned | 2011-12-05T21:33:11Z | |
dc.date.available | 2011-12-05T21:33:11Z | |
dc.date.issued | 2011-07 | |
dc.date.submitted | 2010-11 | |
dc.identifier.issn | 1091-6490 | |
dc.identifier.uri | http://hdl.handle.net/1721.1/67447 | |
dc.description.abstract | The parallel beta-helix is a geometrically regular fold commonly found in the proteomes of bacteria, viruses, fungi, archaea, and some vertebrates. beta-helix structure has been observed in monomeric units of some aggregated amyloid fibers. In contrast, soluble beta-helices, both right- and left-handed, are usually “capped” on each end by one or more secondary structures. Here, an in-depth classification of the diverse range of beta-helix cap structures reveals subtle commonalities in structural components and in interactions with the beta-helix core. Based on these uncovered commonalities, a toolkit of automated predictors was developed for the two distinct types of cap structures. In vitro deletion of the toolkit-predicted C-terminal cap from the pertactin beta-helix resulted in increased aggregation and the formation of soluble oligomeric species. These results suggest that beta-helix cap motifs can prevent specific, beta-sheet-mediated oligomeric interactions, similar to those observed in amyloid formation. | en_US |
dc.description.sponsorship | National Institutes of Health (U.S.) (NIH grant U54-LM008748) | en_US |
dc.description.sponsorship | National Institutes of Health (U.S.) (NIH grant R01-GM25874) | en_US |
dc.description.sponsorship | National Institutes of Health (U.S.) (NIH grant R01GM081871) | en_US |
dc.language.iso | en_US | |
dc.publisher | National Academy of Sciences (U.S.) | en_US |
dc.relation.isversionof | http://dx.doi.org/10.1073/pnas.1017504108 | en_US |
dc.rights | Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. | en_US |
dc.source | PNAS | en_US |
dc.title | Structure-based prediction reveals capping motifs that inhibit beta-helix aggregation | en_US |
dc.title.alternative | Structure-based prediction reveals capping motifs that inhibit β-helix aggregation | en_US |
dc.type | Article | en_US |
dc.identifier.citation | Bryan, A. W. et al. “Structure-based prediction reveals capping motifs that inhibit beta-helix aggregation.” Proceedings of the National Academy of Sciences 108.27 (2011): 11099-11104. | en_US |
dc.contributor.department | Harvard University--MIT Division of Health Sciences and Technology | en_US |
dc.contributor.department | Massachusetts Institute of Technology. Computer Science and Artificial Intelligence Laboratory | en_US |
dc.contributor.department | Massachusetts Institute of Technology. Department of Materials Science and Engineering | en_US |
dc.contributor.department | Massachusetts Institute of Technology. Department of Mathematics | en_US |
dc.contributor.department | Whitehead Institute for Biomedical Research | en_US |
dc.contributor.approver | Berger, Bonnie | |
dc.contributor.mitauthor | Berger, Bonnie | |
dc.contributor.mitauthor | Bryan, Allen W. | |
dc.contributor.mitauthor | Hosur, Raghavendra | |
dc.relation.journal | Proceedings of the National Academy of Sciences of the United States of America | en_US |
dc.eprint.version | Final published version | en_US |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | en_US |
eprint.status | http://purl.org/eprint/status/PeerReviewed | en_US |
dspace.orderedauthors | Bryan, A. W.; Starner-Kreinbrink, J. L.; Hosur, R.; Clark, P. L.; Berger, B. | en |
dc.identifier.orcid | https://orcid.org/0000-0002-2724-7228 | |
mit.license | PUBLISHER_POLICY | en_US |
mit.metadata.status | Complete | |