Paradigms are meant to be broken. In the 1980s, biology students were taught "the one gene = one protein" dogma which has since stepped down from its pedestal, as we now know that one gene, by way of any number of post-translational modifications on the protein sequence, can actually give rise to more than one protein. Or what would be more correct: to more than one function. In the same way, structural biologists are beginning to realise that proteins are not always stable but that a significant amount exist in particularly unstable forms - which has given them the name "disordered proteins". Until recently, proteins were thought to fold up into thermodynamically stable forms before getting on with what they had to do. Now we know that it is not necessarily the case. Eukaryotic translation initiation factor 4E-binding protein 2, for instance, is one such disordered protein whose lack of stability gives rise to a new kind of biological regulation.
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Snapshot : poliovirus receptor
All organisms need other organisms to survive. Flowers need bees. Frogs need flies. Humans need fruit. And viruses need us. As an example, poliovirus invades human cells where it can use what it needs to replicate and multiply. In doing so, the virus not only damages the host cell but also interferes with its activity. However, before a virus stands a chance of invading a cell, let alone propagating inside it, something has to let it in. For poliovirus, that something is a protein receptor, known as the poliovirus receptor. These receptors are found on the surface of cells and are specifically recognised by poliovirus, which docks to them and then finds a way to wriggle inside the cell.
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