Dear colleagues We have been working on a protein that is produced as a pro-peptide, cleaved internally and reassembled into a complex. The interacting regions are the new C and N-termini at the cleavage site, so no rearrangement or loss of part of the protein is involved. The resulting interacting region is quite intricate, with a helix bundle and beta-sheet composed of members of each partner protein.
I wonder if there are other examples of such processing required for folding/assembly of a functional complex? I'm not talking of processing involving removal of termini or internal regions like signal removal in transported proteins or maturation of preproinsulin, for example. I'm interested in examples where a propeptide is cleaved, then the two proteins reassemble in a complex via interactions of the similarly oriented new termini. Any suggestions most appreciated. Thanks a lot! Paula ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1
