Self-organization and regulation of intrinsically disordered proteins with folded N-termini
Here we hypothesize that some proteins use their structured N-terminal domains (SNTDs) to organize the remaining protein chain by means of intramolecular interactions, so generating partially condensed proteins. This model has several attractive features: as the nascent protein chain emerges from th...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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Public Library of Science
2011
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| _version_ | 1826256588827000832 |
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| author | Simister, P Schaper, F O'Reilly, N McGowan, S Feller, S |
| author_facet | Simister, P Schaper, F O'Reilly, N McGowan, S Feller, S |
| author_sort | Simister, P |
| collection | OXFORD |
| description | Here we hypothesize that some proteins use their structured N-terminal domains (SNTDs) to organize the remaining protein chain by means of intramolecular interactions, so generating partially condensed proteins. This model has several attractive features: as the nascent protein chain emerges from the ribosome, the SNTD folds spontaneously and then serves as a nucleation point for the yet unstructured amino acid chain, creating more compact shapes. This reduces the risk of protein degradation or aggregation. Moreover, an interspersed pattern of SNTD-docked regions and free loops can coordinate assembly of sub-complexes in defined loop-sections and enables novel regulatory mechanisms, for example through posttranslational modifications of docked regions. |
| first_indexed | 2024-03-06T18:04:37Z |
| format | Journal article |
| id | oxford-uuid:01042d19-5aa3-4c3b-99db-2467efd3140b |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:04:37Z |
| publishDate | 2011 |
| publisher | Public Library of Science |
| record_format | dspace |
| spelling | oxford-uuid:01042d19-5aa3-4c3b-99db-2467efd3140b2022-03-26T08:32:30ZSelf-organization and regulation of intrinsically disordered proteins with folded N-terminiJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:01042d19-5aa3-4c3b-99db-2467efd3140bEnglishSymplectic Elements at OxfordPublic Library of Science2011Simister, PSchaper, FO'Reilly, NMcGowan, SFeller, SHere we hypothesize that some proteins use their structured N-terminal domains (SNTDs) to organize the remaining protein chain by means of intramolecular interactions, so generating partially condensed proteins. This model has several attractive features: as the nascent protein chain emerges from the ribosome, the SNTD folds spontaneously and then serves as a nucleation point for the yet unstructured amino acid chain, creating more compact shapes. This reduces the risk of protein degradation or aggregation. Moreover, an interspersed pattern of SNTD-docked regions and free loops can coordinate assembly of sub-complexes in defined loop-sections and enables novel regulatory mechanisms, for example through posttranslational modifications of docked regions. |
| spellingShingle | Simister, P Schaper, F O'Reilly, N McGowan, S Feller, S Self-organization and regulation of intrinsically disordered proteins with folded N-termini |
| title | Self-organization and regulation of intrinsically disordered proteins with folded N-termini |
| title_full | Self-organization and regulation of intrinsically disordered proteins with folded N-termini |
| title_fullStr | Self-organization and regulation of intrinsically disordered proteins with folded N-termini |
| title_full_unstemmed | Self-organization and regulation of intrinsically disordered proteins with folded N-termini |
| title_short | Self-organization and regulation of intrinsically disordered proteins with folded N-termini |
| title_sort | self organization and regulation of intrinsically disordered proteins with folded n termini |
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