Candidates for these binding partners are the BH3-only proteins, which like BIM, have been shown to have higher affinities for anti-apoptotic BCL2 family members and can only bind weakly to BAX [ 30].
The oncogenic functions of E6 occur through its interaction with a number of cellular regulatory proteins and one of the best characterized E6-binding partners is the E6-associated protein (E6-AP) [ 7, 8].
Indeed, E6 is a multifunctional protein, and a large number of cellular proteins have been found to interact with it; among the most well-known binding partners is p53, the tumor suppressor, which it targets for proteasome-mediated degradation [ 10].
The notation of these binding partners is analogous to the notation of species, however, the binding partners do not have to be defined in the section #molecules.
Elucidation of the fine molecular mechanisms of arrestin-1 interactions with rhodopsin and other binding partners is necessary for the comprehensive understanding of rod function and for devising novel molecular tools and therapeutic approaches to the treatment of visual disorders.
The specificity of motif binding, accessibility of recognition sites, and expression of cell-type restricted cooperative binding partners, is believed to determine the fidelity of the transcriptional response (e.g. [ 3– 5]).
The hypothesis that there are more, as yet unidentified, binding partners is particularly appealing, given the poor activity of even the wild-type mtPAP when assayed, in vitro.
In this case, almost trivially, the finding of the binding partners is enabled by a non-specific element encoded in their respective structures – the hydrophobicity of their overall molecular surface.
