engleski

Non-specific component of protein-protein interactions

Protein-protein interactions (PPI) are the central pillar supporting most of biological functional activity on the molecular level. A binding event between two proteins typically consists of two stages: 1) diffusional search of the binding partners for each other, and 2) specific recognition of the compatible binding surfaces followed by the formation of the complex We focus here on the non-specific component of PPI, which refers to all physico-chemical properties of the binding partners (such as size, charge, isoeletric point, hydrophilicity etc.) that are independent of the exact dertails of their binding sites, but could in turn affect their localization or diffusional search for one another. It is known that proteins can co-localize due to segregation into different cellular compartments, sequestration via anchor and acaffold proteins or even chemical modifications. We suggest that the non-specific component of PPI determines in part the co-localization and clustering of the binding partners, which then directly in a non-specific fashion influences their interactions. We examine the possibility that such signature might be encoded within the experimental 3D structurtes of a large set of known mutually interacting proteins. We provide preliminary evidence that this indeed may be the case, and corroborate our findings by using different statistical test to compare those features of the known interacting partners, and ascertain correlations and commonlities between them.

protein-protein interactions; physico-chemical properties; interacting partners

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