Hi Natalia, This might be a good place to start:
http://www.sciencedirect.com/science/article/pii/S0968000404002348 The power of two: protein dimerization in biology. Trends Biochem Sci. 2004 Nov;29(11):618-25 Marianayagam NJ1, Sunde M, Matthews JM. Abstract: The self-association of proteins to form dimers and higher-order oligomers is a very common phenomenon. Recent structural and biophysical studies show that protein dimerization or oligomerization is a key factor in the regulation of proteins such as enzymes, ion channels, receptors and transcription factors. In addition, self-association can help to minimize genome size, while maintaining the advantages of modular complex formation. Oligomerization, however, can also have deleterious consequences when nonnative oligomers associated with pathogenic states are generated. Specific protein dimerization is integral to biological function, structure and control, and must be under substantial selection pressure to be maintained with such frequency throughout biology. Shane On Wed, Apr 8, 2015 at 11:59 AM, Natalia O <natalie.c...@gmail.com> wrote: > Dear All, > > > > I have a question that is a little bit related to the previous discussion > about crystallisation of a minority fraction monomers. I wonder if there is > a review of some sort (or anything in principle) that would discuss role of > dimerization (or more broadly oligomerization) in proteins in general. It’s > clear that dimerization can be used for regulation (only one species is > active), but for other dimers this on/off mechanism is not important. I’m > just curious if someone did any comparisons… > > > > > > Thank you! > > > > Natalia >
