Abstract
Thousands of human proteins lack recognizable tertiary structure in most of their chains. Here we hypothesize that some use their structured N-terminal domains (SNTDs) to organise the remaining protein chain via intramolecular interactions, generating partially structured proteins. This model has several attractive features: as protein chains emerge, SNTDs form spontaneously and serve as nucleation points, 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.
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Simister, P., Schaper, F., O'Reilly, N. et al. Self-organization of intrinsically disordered proteins with folded N-termini . Nat Prec (2010). https://doi.org/10.1038/npre.2010.5124.1
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DOI: https://doi.org/10.1038/npre.2010.5124.1