Title |
Prediction of protein interaction types based on sequence and network features
|
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Published in |
BMC Systems Biology, December 2013
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DOI | 10.1186/1752-0509-7-s6-s5 |
Pubmed ID | |
Authors |
Florian Goebels, Dmitrij Frishman |
Abstract |
Protein interactions mediate a wide spectrum of functions in various cellular contexts. Functional versatility of protein complexes is due to a broad range of structural adaptations that determine their binding affinity, the number of interaction sites, and the lifetime. In terms of stability it has become customary to distinguish between obligate and non-obligate interactions dependent on whether or not the protomers can exist independently. In terms of spatio-temporal control protein interactions can be either simultaneously possible (SP) or mutually exclusive (ME). In the former case a network hub interacts with several proteins at the same time, offering each of them a separate interface, while in the latter case the hub interacts with its partners one at a time via the same binding site. So far different types of interactions were distinguished based on the properties of the corresponding binding interfaces derived from known three-dimensional structures of protein complexes. |
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