Abstract
AbstractThousands 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.
Highlights
Proteins were for a long time thought to be mostly well-structured entities made up of one or several domains, which are assembled from spontaneously forming α-helices and/or β-strands, or are folded with the help of chaperones
Structural disorder appears to serve only as a weak signal for intracellular protein degradation and intrinsically disordered’ (ID)-proteins do not appear to display an overall preference for chaperone binding in vivo [17], despite the prominent role that chaperones clearly play in supporting protein folding in general [18]
We suggest here a further novel mechanism for rapidly establishing a certain degree of order within long ID protein chains
Summary
Proteins were for a long time thought to be mostly well-structured entities made up of one or several domains, which are assembled from spontaneously forming α-helices and/or β-strands, or are folded with the help of chaperones. ID proteins have important functions in multi-protein complex assembly and cell signaling [4 - 7] and we need to learn much more about their molecular activities and mechanisms of action.
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