Dear ccp4bb members, A quick off topic question. I have a protein whose domain structure runs N-TM-receptor-TM-enzyme-C, i.e. is a two transmembrane-helix containing signalling protein. One would suspect that the receptor domain has ends that cluster, and that the enzyme (via homology with known systems) is activated when the two helices self-interact in a dimeric protein as a four helix bundle.
So...my question - I have tried expressing the receptor domain as a soluble protein, it works well, folds, purifies, but doesn't crystallize. Does anyone know of an example of taking an exposed membrane protein loop/domain and making a chimera with a soluble 4 helix bundle such that the ends of the loop are tethered and restrained nicely? I was thinking that this must've been attempted for transmembrane alpha-helical signalling proteins, perhaps even "PDB output" successfully! Best Andy ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1
